Affinage

GBF1

Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 · UniProt Q92538

Length
1860 aa
Mass
206.6 kDa
Annotated
2026-06-10
79 papers in source corpus 52 papers cited in narrative 53 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

GBF1 is a large, multi-domain Sec7-family guanine nucleotide exchange factor that drives early secretory traffic by activating ARF GTPases on cis-Golgi and pre-Golgi membranes to nucleate COPI coat recruitment (PMID:10402461, PMID:16890159, PMID:18003980). It cycles rapidly between cytosol and Golgi membranes (membrane half-life on the order of seconds), and each membrane-association event catalyzes a single ARF activation, with GBF1's own catalytic GDP-to-GTP exchange triggering its release; the BFA-stabilized ARF-GDP–GEF complex traps GBF1 on membranes by blocking this catalytic cycle (PMID:15616190, PMID:15813748). Membrane recruitment depends on the C-terminal HDS1/HDS2 region binding a heat-labile Golgi protein receptor and PI4P generated by PI4KIIIα, is regulated by localized ARF-GDP, and is promoted by the GBF1 effector Rab1b (PMID:17429068, PMID:20530568, PMID:29507113, PMID:23943872). Functionally, GBF1 is required for COPI-dependent transmembrane (but not soluble) cargo trafficking and Golgi subcompartmentalization; its loss tubulates the cis-Golgi, disperses COPI, and triggers an ER-stress/UPR program rather than Golgi collapse into ER (PMID:18003980, PMID:17956946, PMID:18287014). GBF1 also feeds a GEF cascade in which its ARF4/ARF5 products recruit BIG1/BIG2 and GGA adaptors at the TGN to direct clathrin-coated, lysosomal-cargo sorting (PMID:23386609, PMID:17666033), and it organizes mitochondrial positioning through ARF1 and the mitochondrial protein Miro via dynein-dependent retrograde transport (PMID:30459446). GBF1 activity is gated by phosphorylation that couples trafficking to cell state: CDK1-cyclin B and AMPK phosphorylation dissociate GBF1 from the Golgi to drive mitotic Golgi disassembly, CK2 phosphorylation at Ser292/Ser297 targets GBF1 to SCFβTrCP for degradation enabling postmitotic Golgi reformation and cytokinesis, AMPK phosphorylation at Thr1337 fragments the Golgi under energy stress, and Src phosphorylation at Y876/Y898 promotes ARF1 binding and retrograde Golgi-to-ER tubular transport of glycosylation enzymes (PMID:20175751, PMID:23418352, PMID:29898406, PMID:39575556, PMID:34870592). A missense mutation in the HDS2 domain abolishes Golgi recruitment and ARF1 activation, causing ER-stress-driven endothelial apoptosis and vascular hemorrhage in zebrafish, and a heterozygous GBF1 mutation reducing protein levels produces UPR activation and a cataract phenotype, establishing GBF1 dysfunction as disease-causing (PMID:28003365, PMID:39110251). Numerous RNA viruses co-opt GBF1 for replication-complex biogenesis: enterovirus 3A proteins directly bind and sequester GBF1 to block ARF1 activation, while diverse viruses (HCV, coronaviruses, dengue, others) depend on GBF1 activity—sometimes through its noncatalytic C-terminal domains independently of the canonical Sec7 COPI function (PMID:16890159, PMID:18551169, PMID:19906930, PMID:20497182, PMID:30567983, PMID:31375590).

Mechanistic history

Synthesis pass · year-by-year structured walk · 23 steps
  1. 1998 Medium

    Establishing the molecular identity of GBF1 was the prerequisite for any mechanistic work, defining it as a ubiquitously expressed Sec7-domain protein with a distinct domain architecture.

    Evidence cDNA cloning, Northern blotting, and chromosomal mapping of human GBF1

    PMID:9828135

    Open questions at the time
    • No enzymatic activity or substrate demonstrated
    • No localization or trafficking role established
  2. 1999 High

    The question of what GBF1 does biochemically was answered by showing it is a BFA-resistant ARF GEF on Golgi membranes, placing it in the COPI/ARF activation machinery.

    Evidence Expression cloning with in vitro GEF assay, immunogold EM, and overexpression conferring BFA-resistant Golgi morphology

    PMID:10402461

    Open questions at the time
    • In vitro specificity (ARF5) did not resolve the physiological substrate
    • Mechanism of membrane recruitment unknown
  3. 2003 High

    Identifying p115 as a proline-rich-region partner connected GBF1 to membrane tethering, though it showed targeting of neither protein depends on the interaction.

    Evidence Yeast two-hybrid, in vitro binding, co-IP, and dominant-negative domain expression

    PMID:12634853

    Open questions at the time
    • Functional consequence of the GBF1–p115 interaction for trafficking not defined
    • Single lab
  4. 2005 High

    Live-imaging and dominant-negative mutants resolved the catalytic cycle question: GBF1 turns over on membranes in seconds and its own exchange activity drives its release, defining one GBF1-membrane event per ARF activation.

    Evidence GFP-GBF1 FRAP with catalytically inactive E794K and ARF1-T31N mutants and BFA treatment

    PMID:15616190 PMID:15813748

    Open questions at the time
    • Identity of the membrane recruitment receptor unknown
    • How catalysis triggers conformational release not structurally defined
  5. 2006 High

    Antibody microinjection directly linked GBF1 to COPI (but not COPII) recruitment in the early secretory pathway, distinguishing its compartment of action.

    Evidence GFP-GBF1 live imaging and anti-GBF1 antibody microinjection with COPI/COPII readouts

    PMID:16926190

    Open questions at the time
    • ARF isoform(s) activated in vivo not pinned down
    • Recruitment determinants not mapped
  6. 2007 High

    siRNA and structural domain studies clarified that GBF1 specifically governs cis-Golgi COPI and transmembrane (not soluble) cargo traffic, that DCB/HUS domains mediate dimerization, and that loss triggers UPR rather than Golgi-to-ER collapse.

    Evidence siRNA depletion with cargo trafficking assays, DCB/HUS domain biochemistry and yeast complementation, and proteomic UPR analysis

    PMID:17640864 PMID:17956946 PMID:18003980 PMID:18287014

    Open questions at the time
    • Basis of transmembrane vs soluble cargo selectivity unresolved
    • Mechanistic link from GBF1 loss to S2P/ATF6 activation not fully defined
  7. 2007 High

    Discovery of Rab1b and GGA interactions positioned GBF1 within an upstream regulatory and downstream adaptor network for membrane recruitment and lysosomal cargo sorting.

    Evidence Co-IP, FRAP, and siRNA for Rab1b effector role and GGA recruitment/cargo trafficking

    PMID:17429068 PMID:17666033

    Open questions at the time
    • How Rab1b mechanistically stabilizes GBF1 not resolved here
    • Direct vs indirect nature of GGA recruitment unclear
  8. 2006 High

    Enterovirus 3A proteins were shown to directly target GBF1, establishing GBF1 as a host factor co-opted/inhibited by viruses and providing a tool to dissect GBF1 domains.

    Evidence Co-IP, COPI recruitment and transport assays, chimeric 3A swaps, and mouse virulence

    PMID:16890159 PMID:17005635 PMID:17329336

    Open questions at the time
    • Structural basis of the 3A–GBF1 N-terminal interaction not solved
    • Whether 3A binding fully recapitulates physiological GBF1 regulation unclear
  9. 2009 High

    Multiple virus systems established that GBF1 is required for RNA replication, and that some viruses use GBF1 functions distinct from canonical COPI-vesicle formation.

    Evidence siRNA, Golgicide A, BFA-resistant GBF1 rescue, and replicon assays across CVB3 and HCV

    PMID:19740986 PMID:19906930

    Open questions at the time
    • Precise GBF1 activity required at the replication complex not defined
    • Whether ARF activation is always the operative step unclear
  10. 2010 High

    Domain-dissection rescue of poliovirus replication by the noncatalytic GBF1 N-terminus revealed a Sec7-independent viral support function, separating GBF1's trafficking role from its viral role.

    Evidence BFA-resistant N-terminal fragment rescue and p115/Rab1b knockdown in poliovirus replication

    PMID:20497182

    Open questions at the time
    • Molecular activity of the N-terminal fragment at replication sites unknown
    • How GBF1 supports replication without exchange activity unresolved
  11. 2010 Medium

    Identification of PI4KIIIα/PI4P as a recruitment requirement and CDK1-cyclin B as a mitotic kinase began to explain how GBF1 membrane association is spatially and cell-cycle regulated.

    Evidence PI4P inhibitors/biosensor and PI4KIIIα depletion; in vitro CDK1 kinase assay with fractionation

    PMID:20175751 PMID:20530568

    Open questions at the time
    • Whether PI4P binding is direct to GBF1 not shown
    • CDK1 phosphosites not fully mapped to mechanism
  12. 2013 High

    Biochemical reconstitution localized lipid-binding to an HDS1 amphipathic helix and showed the Sec7 domain restrains it, defining how GBF1 engages Golgi membranes and lipid droplets.

    Evidence In vitro liposome/artificial lipid droplet binding with domain mutagenesis validated in cells

    PMID:21789191 PMID:23943872

    Open questions at the time
    • Identity of the proteinaceous Golgi receptor still unknown at this stage
    • Regulation of HDS1 exposure in the full-length protein unresolved
  13. 2013 High

    Epistasis placed GBF1 upstream of BIG1/BIG2 via ARF4/ARF5, defining a GEF cascade extending GBF1's reach to the TGN clathrin-adaptor machinery.

    Evidence ARF isoform-specific siRNA epistasis and immunoEM localization across Golgi compartments

    PMID:23386609

    Open questions at the time
    • Direct vs indirect basis of BIG recruitment by ARF4/5 not biochemically resolved
    • Spatial organization of the cascade not defined
  14. 2013 Medium

    AMPK phosphorylation of GBF1 during mitosis was identified as an energy- and cell-cycle-coupled control of GBF1 membrane association and Golgi disassembly.

    Evidence Cell synchronization, AMPK kinase assays on GBF1, and Golgi fragmentation readouts

    PMID:23418352

    Open questions at the time
    • Phosphosite not mapped in this study
    • Mechanism by which phosphorylation abolishes GEF activity unclear
  15. 2016 High

    A zebrafish HDS2 missense mutation tied loss of Golgi recruitment and ARF1 activation to ER-stress-driven endothelial apoptosis, providing in vivo disease-relevant proof of GBF1's secretory function.

    Evidence ENU screen, positional cloning, and cell-based Golgi recruitment/ARF1/COPI assays with ER-stress markers and rescue

    PMID:28003365

    Open questions at the time
    • Whether the human ortholog causes analogous vascular disease not addressed
    • Precise HDS2 recruitment mechanism not structurally defined
  16. 2018 High

    An in vitro recruitment assay plus domain mapping established that HDS1/HDS2 and a heat-labile Golgi protein receptor, gated by ARF-GDP localization, control GBF1 membrane association.

    Evidence In vitro Golgi-membrane recruitment assay, truncation analysis, protease/heat treatment, and ArfGAP siRNA

    PMID:29443553 PMID:29507113

    Open questions at the time
    • Molecular identity of the Golgi receptor not determined
    • How ARF-GDP localization is read out by GBF1 unresolved
  17. 2018 High

    CK2-dependent phosphorylation at Ser292/Ser297 was shown to recruit βTrCP and target GBF1 for SCFβTrCP degradation, coupling GBF1 turnover to postmitotic Golgi reformation and cytokinesis.

    Evidence Phosphosite mapping, CK2 kinase assay, βTrCP co-IP, ubiquitin ligase assay, and non-degradable mutant phenotypes

    PMID:29898406

    Open questions at the time
    • How localized degradation at the intercellular bridge is spatially restricted not fully defined
    • Interplay with other mitotic phospho-controls unresolved
  18. 2018 High

    Reciprocal co-IP and live imaging revealed that GBF1–ARF1–Miro controls mitochondrial positioning, extending GBF1 function beyond classical secretory traffic.

    Evidence GBF1–Miro and ARF1–Miro co-IP, GBF1 inhibition, dynein/Miro perturbation, and mitochondrial movement tracking

    PMID:30459446

    Open questions at the time
    • Whether GBF1 acts on Miro directly or via ARF1 effectors unclear
    • Connection to canonical Golgi pool not defined
  19. 2019 Medium

    Proximity proteomics and direct interaction studies expanded the GBF1 interactome (C10orf76, HCV NS3) and linked AMPK-GBF1 to physiological cargo (VWF, ECM) trafficking.

    Evidence BioID/MS with co-IP and FRAP for C10orf76; Y2H/co-IP/PLA for NS3; trafficking assays with AMPK/glucose manipulation for VWF

    PMID:30567983 PMID:31056345 PMID:31519766

    Open questions at the time
    • Mechanistic role of C10orf76 in GBF1 recruitment incompletely defined
    • AMPK phosphosite governing VWF trafficking not mapped here
  20. 2021 High

    Src phosphorylation of GBF1 at Y876/Y898 was shown to promote ARF1 binding and drive retrograde tubular transport of glycosylation enzymes, defining a phospho-switch that redirects GBF1 output.

    Evidence Src kinase assay, phosphopeptide MS, GBF1–ARF1 co-IP, phosphomimetic/deficient mutants, live imaging, and molecular modeling

    PMID:34870592

    Open questions at the time
    • Structural model of Sec7 melting awaits experimental structure
    • How retrograde vs anterograde decision is integrated with other phospho-inputs unclear
  21. 2024 High

    CRISPR knock-in of a phospho-deficient GBF1-T1337A mutant established AMPK-Thr1337 phosphorylation as the operative event for energy-stress Golgi fragmentation and slowed anterograde traffic.

    Evidence AMPK-α knockouts, GBF1-T1337A knock-in, AMPK activators, and Golgi fragmentation/cargo trafficking assays

    PMID:39575556

    Open questions at the time
    • How a single phosphosite triggers Golgi fragmentation mechanistically not resolved
    • Relationship of Thr1337 to mitotic AMPK control unclear
  22. 2024 Medium

    Separation-of-function phosphomutants and a human mutation/knockout mouse linked GBF1 to distinct cytokinesis vs secretion roles and to UPR/autophagy and a cataract disease phenotype.

    Evidence Phosphomimetic/deficient mutagenesis with cytokinesis/Golgi assays; knockdown with XBP1s/autophagy readouts and Gbf1 heterozygous knockout mice

    PMID:37604968 PMID:39110251

    Open questions at the time
    • Interaction networks distinguishing the two functional modes not fully identified
    • Causal chain from reduced GBF1 to cataract not mechanistically complete
  23. 2024 Medium

    Enterovirus 3A sequestration of GBF1 was shown to induce PERK/CHOP-driven ER stress and apoptosis, and synthetic lethality screening identified ARF1 as the dominant dependency of GBF1 hypomorphism.

    Evidence 3A expression with co-IP/ARF1 activation, UPR markers, PERK inhibitor rescue; synthetic lethality screen with ARF1 disruption in 3A-expressing cells

    PMID:36305789 PMID:38904364

    Open questions at the time
    • Whether ARF1 is the sole essential GBF1 substrate in all contexts unclear
    • Generality of PERK/CHOP induction across GBF1 loss-of-function modes not established

Open questions

Synthesis pass · forward-looking unresolved questions
  • The identity of the heat-labile Golgi protein receptor that recruits GBF1 and a high-resolution structure of full-length GBF1 explaining how phosphorylation and lipid binding gate Sec7 catalysis remain unresolved.
  • No molecular identity for the Golgi recruitment receptor
  • No experimental full-length or Sec7-conformational structure tying phospho-switches to catalysis
  • Integration of the many phospho-inputs into a unified regulatory logic not established

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 4 GO:0008289 lipid binding 3 GO:0060090 molecular adaptor activity 2
Localization
GO:0005794 Golgi apparatus 5 GO:0005829 cytosol 3 GO:0005783 endoplasmic reticulum 2 GO:0005811 lipid droplet 2
Pathway
R-HSA-1643685 Disease 5 R-HSA-1640170 Cell Cycle 4 R-HSA-5653656 Vesicle-mediated transport 4 R-HSA-8953897 Cellular responses to stimuli 4 R-HSA-9609507 Protein localization 3
Partners
ARF1ARF4ATGLC10ORF76MIROP115RAB1B
Complex memberships
GBF1–Arf4–rhodopsin complexSCFβTrCP (substrate)

Evidence

Reading pass · 53 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 GBF1 was identified as a novel Golgi-associated guanine nucleotide exchange factor (GEF) with a Sec7 domain that exhibits BFA-resistant guanine nucleotide exchange activity with apparent specificity toward ARF5 at physiological Mg2+ concentrations. Overexpression conferred BFA resistance on Golgi morphology and ARF activation/COPI recruitment. GBF1 is primarily cytosolic but a significant pool co-localizes with COPI beta-subunit at a perinuclear structure and by immunogold labeling to Golgi cisternae and smooth vesiculotubular structures. Expression cloning, hexahistidine-tagged in vitro GEF activity assay, immunofluorescence, immunogold EM, subcellular fractionation The Journal of cell biology High 10402461
1998 Human GBF1 encodes a 206.5 kDa protein containing a centrally positioned Sec7 domain and a proline-rich C-terminal region. Its mRNA is expressed ubiquitously across 17 tissues. The gene maps to chromosomal locus 10q24 and the Sec7 domain-encoding region harbors four introns. cDNA cloning, Northern blotting, chromosomal mapping (YAC, radiation hybrid) Genomics Medium 9828135
2003 GBF1 physically interacts with the membrane-tethering protein p115 through the proline-rich region of GBF1 and the head region of p115. The interaction was identified by yeast two-hybrid and confirmed by in vitro binding and co-immunoprecipitation. The two proteins co-localize in the Golgi and peripheral VTCs. Expression of the p115-binding (pro-rich) region of GBF1 caused Golgi disruption, demonstrating functional relevance, but the interaction was not required for targeting either protein to membranes. Yeast two-hybrid screen, in vitro binding assay, co-immunoprecipitation, immunofluorescence, domain mutagenesis EMBO reports High 12634853
2004 GBF1 cycles rapidly on and off Golgi membranes (fast turnover by FRAP), and BFA, which forms an Arf-GDP–GEF inhibitory complex, stabilizes GBF1 on Golgi membranes. Using an in vivo Arf1-GTP reporter assay, GBF1 exchange activity on Arf1 was shown to be inhibited by BFA in mammalian cells, consistent with formation of an Arf1–GBF1–BFA ternary complex with longer membrane residence. YFP-GBF1 FRAP, in vivo Arf1-GTP level assay, BFA treatment Molecular biology of the cell High 15616190
2005 GBF1 rapidly cycles between membranes and cytosol with t½ ~17 s. GBF1 is stabilized on membranes when complexed with ARF-GDP (shown by inactive E794K GBF1 mutant, ARF1-T31N mutant, or BFA). GBF1 dissociation from ARF and membranes is triggered by its catalytic activity (GDP displacement and GTP binding to ARF), implying that each GBF1 membrane association catalyzes a single ARF activation event. GFP-GBF1 FRAP, expression of catalytically inactive GBF1-E794K mutant, ARF1-T31N expression, BFA treatment Traffic (Copenhagen, Denmark) High 15813748
2006 GBF1 localizes to both Golgi membranes and peripheral puncta near but separate from ER exit sites, associating dynamically with both. BFA causes accumulation of GBF1 on these membranes before redistribution to ER in a microtubule-dependent manner. Microinjection of anti-GBF1 antibodies specifically caused dissociation of COPI from membranes, demonstrating that GBF1 regulates COPI membrane recruitment in the early secretory pathway. GBF1 recruitment to cargo-containing peripheral puncta coincided with COPI but not COPII recruitment. GFP-GBF1 live-cell imaging, FRAP, diffusion coefficient measurement, subcellular fractionation, anti-GBF1 antibody microinjection, immunofluorescence Journal of cell science High 16926190
2006 The enterovirus CVB3 3A protein inhibits ARF1 activation by directly binding to GBF1 at its N-terminus, thereby blocking GBF1-mediated COP-I coat complex recruitment to membranes and inhibiting ER-to-Golgi transport. This mechanism is specific to GBF1 (not BIG1/BIG2) and viral mutants defective in this function are less virulent in mice. Co-immunoprecipitation, dominant-negative ARF1 expression, BFA resistance assay in MDCK cells, siRNA knockdown, mouse virulence assay, electron microscopy Developmental cell High 16890159
2006 Among multiple picornavirus 3A proteins tested, only enterovirus (CVB3 and poliovirus) 3A proteins inhibit COP-I recruitment via GBF1 binding. The N-terminal residues of CVB3 3A are critical for GBF1 binding; chimeric HRV 3A proteins with CVB3 N-termini gain the ability to bind GBF1 and inhibit transport. Other picornavirus 3A proteins (HRV, EMCV, FMDV, HAV) fail to bind GBF1 or inhibit COP-I recruitment. Co-immunoprecipitation, COP-I recruitment assay, protein transport assay, chimeric protein analysis Journal of virology High 17005635
2007 The 3A protein of CVB3 must form homodimers to bind GBF1 and trap it on membranes. A conserved region in the N-terminus of 3A is required for GBF1 binding but not dimerization. In GBF1, the extreme N-terminus, the dimerization/cyclophilin binding (DCB) domain, and the homology upstream of Sec7 (HUS) domain are all required for the interaction with viral 3A. A GBF1 mutant lacking its extreme N-terminus cannot rescue the effects of 3A overexpression. Mutagenesis of 3A and GBF1, co-immunoprecipitation, functional rescue assay Journal of virology High 17329336
2007 Rab1b GTPase directly interacts with GBF1 through GBF1's N-terminal domain, identifying GBF1 as a Rab1b effector. Active Rab1b (Rab1bQ67L) increases GBF1 and COPI association with peripheral ER exit site structures, stabilizes Arf1 on Golgi membranes, and Rab1b siRNA reduces GBF1 membrane association. Co-immunoprecipitation, GFP-Rab1b live imaging, FRAP, siRNA knockdown, immunofluorescence Molecular biology of the cell High 17429068
2007 GBF1 colocalizes with GGA adaptor proteins on Golgi membranes and physically interacts with GGAs. Depletion of GBF1 or expression of its inactive mutant prevents GGA recruitment to Golgi membranes and results in improper lysosomal cargo sorting (mannose 6-phosphate receptor and sortilin trafficking). siRNA knockdown, inactive GBF1 mutant expression, co-immunoprecipitation, immunofluorescence, cargo trafficking assay Traffic (Copenhagen, Denmark) Medium 17666033
2007 GBF1 regulates COPI recruitment specifically on cis-Golgi compartments (while BIGs regulate adaptors on trans-Golgi). GBF1 knockdown/COPI knockdown does not prevent ER export of VSVGtsO45 but causes its accumulation in peripheral vesiculotubular clusters, and is required for Golgi subcompartmentalization and cargo progression to the cell surface. GBF1 is required for transmembrane but not soluble protein secretion. siRNA knockdown, VSVGtsO45 trafficking assay, immunofluorescence Molecular biology of the cell High 18003980
2007 siRNA-mediated depletion of GBF1 causes COPI dispersal but, unlike BFA treatment or expression of inactive ARF, does not cause Golgi collapse into ER. Instead, GBF1 depletion causes extensive tubulation of the cis-Golgi with connections to peripheral ERGIC sites. GBF1 depletion dramatically inhibits transmembrane protein trafficking but soluble proteins continue to be secreted, showing cargo-type specificity. siRNA knockdown, live-cell imaging, immunofluorescence, cargo trafficking assays (soluble and transmembrane) Journal of cell science High 17956946
2007 The DCB domains of GBF1, BIG1, and BIG2 mediate homodimerization of each GEF, and an intramolecular interaction between DCB and HUS domains (mediated by the conserved HUS box) determines the architecture of the N-terminal regulatory region. Both DCB and HUS domains are necessary for GBF1 dimerization in mammalian cells, and the DCB domain is essential for yeast viability. Yeast two-hybrid, biochemical pulldown assays, cellular dimerization assay, yeast complementation The Journal of biological chemistry High 17640864
2008 GBF1 depletion by siRNA causes cell-cycle arrest in G0/G1, dispersal of Golgi markers (beta-COP, GM130), induction of ER stress proteins (calreticulin, PDI), and upregulation of UPR chaperones. GBF1 depletion specifically induces relocation of the site-2 protease S2P from Golgi to ER and proteolysis of ATF6, mimicking a UPR response. BIG1 or BIG2 depletion did not reproduce these effects. siRNA knockdown, cell-cycle analysis, immunofluorescence, quantitative proteomics, Western blotting Proceedings of the National Academy of Sciences of the United States of America High 18287014
2008 MHV coronavirus RNA replication requires GBF1-mediated ARF1 activation. Individual siRNA knockdown of GBF1 (but not BIG1 or BIG2) significantly inhibited MHV RNA replication. ARF1 siRNA also inhibited MHV infection. BFA did not block RC formation per se but reduced RC number. MHV was BFA-insensitive in MDCK cells expressing BFA-resistant GBF1. siRNA knockdown (individual targets), BFA pharmacological inhibition in MDCK cells with BFA-resistant GBF1, immunofluorescence, quantitative electron microscopy PLoS pathogens High 18551169
2008 GDP-bound class II Arfs (Arf4, Arf5) associate with ERGIC membranes independently of GBF1. After BFA treatment, Arf1 and Arf3 dissociate from endomembranes while Arf4 and Arf5 persist on ERGIC. A GDP-arrested Arf4(T31N) localizes to ERGIC even with BFA and Exo1 present. Loss of Arf-GTP (by Exo1) causes GBF1 accumulation on Golgi and ERGIC membranes, suggesting GBF1 accumulation can be triggered by loss of Arf-GTP rather than only by Arf-GDP–BFA–GBF1 complex formation. Live-cell imaging of fluorescently tagged Arfs and GBF1, BFA and Exo1 pharmacological treatments, dominant-negative Arf4(T31N) expression Molecular biology of the cell Medium 18524849
2009 CVB3 RNA replication critically requires GBF1. siRNA knockdown of GBF1 inhibited viral RNA replication; overexpression of active but not inactive GBF1 rescued replication in BFA-treated cells. The BFA-resistant GBF1-M832L efficiently rescued both wt and 3A-mutant replicons. BFA-resistant GBF1-A795E rescued wt but not 3A-GBF1 binding-deficient replicons. Overexpression of Arf proteins or Rab1B failed to rescue replication in the presence of BFA. siRNA knockdown, BFA-resistant GBF1 overexpression rescue, subgenomic replicon assay, viral RNA replication quantification Journal of virology High 19740986
2009 GBF1 is required for HCV RNA replication. Individual siRNA knockdown of GBF1 (but not BIG1 or BIG2) and the GBF1-specific inhibitor Golgicide A inhibited HCV replication. Overexpression of BFA-resistant GBF1 rescued HCV replication in BFA-treated cells. BFA did not block membranous web-like structure formation, suggesting GBF1 is involved in replication complex activity rather than formation. siRNA knockdown, specific pharmacological inhibitor (Golgicide A), BFA-resistant GBF1 rescue, immunofluorescence, electron microscopy Journal of virology High 19906930
2009 In Drosophila, garz (the GBF1 ortholog) functions in the pinocytic GEEC (GPI-AP enriched early endosomal compartment) pathway for clathrin-independent endocytosis. Live confocal and TIRF imaging show a fraction of GBF1-GFP dynamically associates with activated Arf1-positive nascent pinosomes. A GTP-exchange-deficient GBF1 mutant impairs fluid phase uptake. GBF1 activation is required for the GEEC pathway even in the presence of BFA, indicating a role in endocytosis separable from its role in secretion. RNAi knockdown in Drosophila cells, live confocal/TIRF imaging, quantitative fluid-phase uptake assay, GTP-exchange-deficient mutant expression PloS one Medium 19707569
2010 For poliovirus replication, GBF1's N-terminal region (lacking the catalytic Sec7 domain) is sufficient to rescue replication in BFA-treated cells. In poliovirus-infected cells, p115 (a normal GBF1 modulator) is degraded and neither p115 nor Rab1b knockdown affects virus replication, indicating that GBF1 supports viral replication through functions distinct from its canonical Arf-activating role in COPI vesicle formation. BFA-resistant GBF1 domain rescue assay (N-terminal fragment lacking Sec7), siRNA knockdown of p115 and Rab1b, viral replication assay Cellular microbiology High 20497182
2010 The phosphatidylinositol 4-kinase PI4KIIIα is required for GBF1 recruitment to Golgi membranes. Inhibitors of PI4P synthesis or depletion of PI4KIIIα prevents GBF1 recruitment to the Golgi. Dominant-active Rab1b increases PI4P levels at the Golgi as detected by GFP-PH sensor, suggesting Rab1b contributes to GBF1 recruitment through activation of PI4KIIIα and subsequent PI4P production. PI4P synthesis inhibitors, siRNA knockdown of PI4KIIIα, GFP-PH PI4P biosensor, dominant-active Rab1b expression, immunofluorescence Journal of cell science Medium 20530568
2010 GBF1 is phosphorylated by CDK1-cyclin B in mitosis, which results in its dissociation from Golgi membranes. This is accompanied by a reduction in membrane-associated GTP-bound ARF in mitotic cells. Despite reduced GBF1 and ARF-GTP, COPI binding to Golgi appears unaffected but remains GBF1-dependent, suggesting a low level of GBF1 activity persists in mitosis. Identification of GBF1 as Golgi phosphoprotein, in vitro kinase assay with CDK1-cyclin B, phosphorylation site mapping, immunofluorescence, membrane fractionation, cell synchronization The Biochemical journal High 20175751
2011 C. trachomatis selectively co-opts GBF1 (not BIG1 or BIG2) for vesicle-mediated sphingomyelin (SM) acquisition. The GBF1/Arf1-dependent pathway provides SM essential for inclusion membrane growth and stability but is not required for bacterial replication. A separate CERT-dependent non-vesicular ceramide transport pathway provides SM required for bacterial replication. siRNA knockdown of individual GEFs, BFA pharmacological inhibition, fluorescent lipid transport assays, inclusion growth/stability quantification, bacterial replication assay PLoS pathogens High 21909260
2011 GBF1 and ATGL (adipose triglyceride lipase) interact directly and in cells. Yeast two-hybrid, co-immunoprecipitation, and direct protein binding assays demonstrate interaction through multiple contact sites. The C-terminal region of ATGL interacts with N-terminal domains of GBF1 including the Sec7 domain (but not full-length GBF1). The ATGL patatin domain interacts with GBF1's HDS1 and HDS2 C-terminal domains. HDS1 and HDS2 expressed alone localize to lipid droplets but not Golgi, unlike full-length GBF1. Yeast two-hybrid, co-immunoprecipitation in mammalian cells, direct protein binding, fluorescence microscopy PloS one Medium 21789191
2012 In Drosophila, loss of garz (GBF1 ortholog) impairs Golgi complex integrity, disrupts vesicle transport of cargo proteins and directed apical membrane delivery, and perturbs polarized epithelial architecture of tubular organs (salivary glands, trachea, proventriculus, hindgut). These phenotypes are caused by dysfunction of the Arf1-COPI machinery. Drosophila loss-of-function mutant analysis (EMS and targeted), immunofluorescence, electron microscopy, cargo trafficking assays in embryos Journal of cell science High 22302994
2012 GBF1 bears a novel phosphatidylinositol-phosphate binding module (BP3K) that binds products of PI3Kγ. Upon GPCR stimulation in neutrophils, GBF1 is translocated from the Golgi to the leading edge to activate Arf1, which recruits p22phox and GIT2 to the leading edge. GBF1-mediated Arf1 activation is required for neutrophil chemotaxis and superoxide production, linking PI3Kγ activity with Arf1 activation. PI3P/PI4P binding assays, immunofluorescence (GBF1 localization on GPCR stimulation), siRNA knockdown, superoxide production assay, chemotaxis assay Molecular biology of the cell Medium 22573891
2012 GBF1 and ARF1 colocalize with PI4KIIIβ at HCV replication complexes. Both ARF1 and GBF1 are required for HCV replication; overexpression of PI4P phosphatase Sac1 inhibits HCV replication. PI4KIIIβ is required for HCV replication and co-localizes with the GBF1/ARF1 machinery, suggesting GBF1/ARF1 generates a PI4P-enriched environment supporting HCV replication. Immunofluorescence co-localization, siRNA knockdown, PI4P phosphatase overexpression, HCV replication assay PloS one Medium 22359663
2013 GBF1-activated ARFs (specifically ARF4 and ARF5, but not ARF3) facilitate BIG1 and BIG2 recruitment to the TGN, establishing a functional cascade between GEFs. GBF1 is ultrastructurally localized to pre-Golgi, Golgi, and also TGN, and its activity at the TGN is required for subsequent BIG1/2 recruitment that coordinates clathrin adaptor coating events. siRNA knockdown, immunofluorescence, ultrastructural localization (immunoelectron microscopy), ARF isoform-specific knockdown The Journal of biological chemistry High 23386609
2013 GBF1 possesses a lipid-binding HDS1 domain immediately downstream of the catalytic Sec7 domain. An amphipathic helix within HDS1 is necessary and sufficient for binding to lipid droplets and Golgi membranes in cells and to bilayer liposomes and artificial lipid droplets in vitro. The catalytic Sec7 domain inhibits the potent lipid-droplet-binding capacity of HDS1. Additional sequences upstream of the Sec7-HDS1 tandem are required for Golgi membrane localization. In vitro liposome binding, in vitro artificial lipid droplet binding, GFP-tagged domain expression in cells, domain deletion/mutagenesis analysis Journal of cell science High 23943872
2013 AMPK is phosphorylated and activated when cells enter mitosis. Activated AMPK phosphorylates GBF1, dissociating GBF1 from Golgi membranes and abolishing its Arf1-GEF activity. AMPK and GBF1 phosphorylation are essential for mitotic Golgi disassembly and subsequent mitosis entry. Cell synchronization, phosphorylation assays, kinase assays (AMPK on GBF1), immunofluorescence, Golgi fragmentation quantification, rescue/inhibition experiments Journal of cell science Medium 23418352
2013 C. elegans GBF-1 localizes to the cis-Golgi and ER-Golgi elements. GBF-1 is required for secretion and Golgi integrity. Additionally, GBF-1 depletion disperses ER reticular structure (without destroying ER exit sites), reduces RAB-5-positive early endosomes, and causes accumulation of RAB-7-positive late endosomes, revealing a role in receptor-mediated endocytosis and endosomal traffic. RNAi knockdown in C. elegans oocytes and intestinal epithelial cells, immunofluorescence/confocal microscopy, endocytosis assays, organelle marker analysis PloS one Medium 23840591
2015 The GBF1-Arf1/Arf4-COPI pathway is necessary for dengue virus capsid transport from the ER membrane to lipid droplets (LDs). This process is independent of COPII components and Golgi integrity. A BFA-resistant form of GBF1 restores capsid distribution in infected cells treated with BFA, demonstrating GBF1 catalytic activity is required. BFA/drug treatment, BFA-resistant GBF1 rescue, COPII/Golgi disruption, immunofluorescence, siRNA knockdown of Arf1/Arf4 Traffic (Copenhagen, Denmark) Medium 26031340
2015 GBF1 oligomerization (mediated by DCB domain residues K91 and E130) is dispensable for Golgi localization, membrane cycling, Arf activation, COPI recruitment, Golgi homeostasis, and cargo secretion, and is not required for poliovirus RNA replication support. However, oligomerization stabilizes GBF1 in cells; the oligomerization-deficient 91/130 mutant is degraded faster than wild-type GBF1. Site-directed mutagenesis, FRAP, ARF activation assay, COPI recruitment assay, secretion assay, poliovirus replication assay, protein stability measurement American journal of physiology. Cell physiology Medium 26718629
2016 In zebrafish, a missense mutation (L1246R) in the HDS2 domain of gbf1 causes vascular hemorrhage. The mutant Gbf1(L1246R) cannot be recruited to the Golgi apparatus and fails to activate Arf1 for COPI complex recruitment, causing ER stress and endothelial apoptosis via PERK/CHOP. Hemorrhage can be partially prevented by ER stress inhibitor tauroursodeoxycholic acid or knockdown of proapoptotic baxb. ENU mutagenesis zebrafish screen, positional cloning, mammalian cell-based Golgi recruitment assay, Arf1 activation assay, COPI recruitment assay, ER stress marker analysis, rescue experiments The Journal of biological chemistry High 28003365
2017 GBF1 forms a functional complex with Arf4 and the photoreceptor cargo rhodopsin at the Golgi/TGN during sensory membrane carrier biogenesis. Rhodopsin and Arf4 bind the regulatory N-terminal DCB-HUS domain of GBF1. The complex is sensitive to Golgicide A (GCA), which blocks rhodopsin delivery to cilia. Newly synthesized rhodopsin in the endomembrane system is essential for GBF1-Arf4 complex formation in vivo. GBF1 also interacts with Arf GAP ASAP1 in a GCA-resistant manner. Co-immunoprecipitation with recombinant human proteins, frog retina in vivo experiments, GCA inhibitor treatment, domain binding mapping Journal of cell science Medium 29025970
2017 GBF1 is involved in the replication of yellow fever virus, Sindbis virus, coxsackievirus B4, and human coronavirus 229E. For HCV and some other viruses, class II Arfs (Arf4/Arf5) downstream of GBF1 are required; for CVB4, no single or paired Arf depletion inhibited replication, suggesting GBF1 supports viral replication through distinct Arf-dependent and Arf-independent mechanisms depending on the virus. siRNA and CRISPR-Cas9 Arf depletion (individual and paired), viral replication assays, GBF1 knockdown The Journal of general virology Medium 29923822
2018 GBF1 and its substrate Arf1 regulate the spatial organization of mitochondria in a microtubule-dependent manner. GBF1 physically interacts with the mitochondrial membrane protein Miro; GTP-bound Arf1 also interacts with Miro. Inhibition of GBF1 causes collapse of the mitochondrial network toward the centrosome through a two-fold increase in time engaged in retrograde movement, dependent on dynein and Miro. GBF1 inhibition also results in larger mitochondria with more complex morphology. Co-immunoprecipitation (GBF1–Miro, Arf1–Miro), GBF1 pharmacological inhibition, immunofluorescence, electron tomography, mitochondrial movement tracking (live imaging), siRNA knockdown of Miro and dynein inhibition Scientific reports High 30459446
2018 GBF1 recruitment to cis-Golgi membranes requires its HDS1 and HDS2 C-terminal domains and a heat-labile, protease-sensitive Golgi-localized protein receptor. Arf-GDP localization is critical for GBF1 recruitment, as a TGN-localized Arf-GDP mutant fails to promote GBF1 recruitment. ArfGAP2 and ArfGAP3 do not contribute to GBF1 recruitment. An in vitro GBF1 recruitment assay was established supporting Arf-GDP regulation of GBF1 membrane association. In vitro GBF1 recruitment assay (Golgi membranes), domain truncation analysis (in vivo and in vitro), heat/protease treatment of Golgi membranes, Arf-GDP localization mutants, ArfGAP siRNA knockdown Journal of cell science High 29507113
2018 Highly conserved residues RDR1168 and LF1266 within α-helices 2 and 6 of the HDS2 domain of GBF1 are critical for GBF1 activity. Alanine substitutions at these positions in BFA-resistant GBF1 compromise Golgi homeostasis, ARF activation, secretion, and cellular viability. These mutations significantly decrease GBF1 Golgi membrane targeting efficiency. BFA-resistant GBF1 replacement assay, alanine-scanning mutagenesis, ARF activation assay, secretion assay, Golgi morphology analysis, Golgi targeting quantification American journal of physiology. Cell physiology Medium 29443553
2018 GBF1 is phosphorylated on Ser292 and Ser297 by casein kinase-2 in mitosis, allowing recognition and binding by the F-box protein βTrCP, which recruits GBF1 to the SCFβTrCP ubiquitin ligase complex and triggers GBF1 degradation. This phosphorylation-dependent degradation occurs along microtubules at the intercellular bridge of telophase cells and is required for Golgi membrane positioning and postmitotic Golgi reformation. A non-degradable GBF1 mutant inhibits Golgi cluster transport and causes cytokinesis failure. Phosphorylation site mapping (Ser292/Ser297), CK2 kinase assay, βTrCP co-immunoprecipitation, SCFβTrCP ubiquitin ligase assay, non-degradable GBF1 mutant expression, immunofluorescence, Golgi inheritance assay, cytokinesis assay Cell reports High 29898406
2019 GBF1 modulates ER-Golgi trafficking of von Willebrand factor (VWF) and extracellular matrix proteins in a selective, limiting-factor manner. GBF1 activation by AMPK couples anterograde trafficking to physiological cues (glucose levels); GBF1 modulates both ER exit and TGN exit of VWF, the latter affecting storage organelle size and hemostatic capacity. AMPK activation of GBF1 links cellular energy status to secretory pathway regulation. Golgi-associated protein screen, GBF1 level modulation, VWF trafficking assay, secretory granule size quantification, AMPK activation/inhibition experiments, glucose manipulation Developmental cell Medium 31056345
2019 C10orf76 is a GBF1 proximal/binding protein identified by BioID proximity biotinylation from enriched Golgi fractions. C10orf76 rapidly cycles on and off GBF1-positive Golgi structures. Its depletion causes Golgi fragmentation, alters GBF1 recruitment to Golgi, and impairs secretion. BioID proximity biotinylation + mass spectrometry from Golgi-enriched fractions, co-immunoprecipitation, siRNA knockdown, FRAP, secretion assay Molecular & cellular proteomics : MCP Medium 31519766
2019 HCV NS3 (protease domain) physically interacts with the Sec7 domain of GBF1. This interaction was demonstrated by yeast two-hybrid, co-immunoprecipitation, and proximity ligation assays. NS3 overexpression interferes with GBF1 function and alters its intracellular localization. A reverse yeast two-hybrid screen identified an NS3 mutant (N77D/S77D) that neither interacts with GBF1 nor supports viral replication despite conserved protease activity, indicating the NS3-GBF1 interaction is required for HCV replication. Yeast two-hybrid (forward and reverse screen), co-immunoprecipitation, proximity ligation assay, NS3 mutagenesis, viral replication assay Journal of virology High 30567983
2019 Multiple GBF1 mutants inactive in cellular trafficking (including Sec7 domain mutants) can still support poliovirus RNA replication. The Arf-activating property (but not specific Sec7 primary structure) is indispensable for viral replication. GBF1 is recruited to replication sites redundantly: via direct interaction with viral 3A protein and via determinants in the noncatalytic C-terminal domains of GBF1. Systematic GBF1 domain mutagenesis, BFA-resistant GBF1 replacement viral replication assay, 3A binding-deficient GBF1 mutant analysis Journal of virology Medium 31375590
2021 Src tyrosine kinase phosphorylates GBF1 on 10 tyrosine residues; phosphorylation of Y876 and Y898 (near the C-terminus of the Sec7 GEF domain) promotes GBF1 binding to Arf1 GTPase. Molecular modeling suggests partial melting of the Sec7 domain and intramolecular rearrangement upon phosphorylation. GBF1 mutants defective for Y876/Y898 phosphorylation prevent Arf1 binding, tubular carrier formation, and GALNTs retrograde relocation; phosphomimetic GBF1 mutants induce retrograde tubules. Src kinase assay, phosphopeptide identification by mass spectrometry, co-immunoprecipitation (GBF1-Arf1), phosphomimetic/phosphodeficient GBF1 mutants, live-cell imaging of retrograde tubules, GALNTs localization assay, molecular modeling eLife High 34870592
2021 GBF1 activity is required for mouse oocyte meiotic maturation. GBF1 localizes to the spindle periphery during metaphase I. Inhibiting GBF1 activity causes aberrant Golgi accumulation around the spindle (condensation of GM130), disrupts ER distribution, induces ER stress (increased GRP78), alters mitochondrial membrane potential, and impairs polar body formation. GBF1 co-localizes with GM130 at the Golgi in oocytes. GBF1 inhibitor treatment (BFA/GCA), immunofluorescence, organelle morphology quantification, mitochondrial membrane potential assay, ER stress marker analysis Microscopy and microanalysis Low 33478608
2022 When poliovirus protein 3A engages GBF1, it renders GBF1 a functional hypomorph. Synthetic lethality screening identified ARF1 as the top synthetic lethal partner of GBF1 loss-of-function; disruption of ARF1 selectively killed cells synthesizing 3A alone or in the context of a poliovirus replicon, while leaving uninfected cells viable. Synthetic lethality screen, siRNA/genetic ARF1 disruption in 3A-expressing vs. uninfected cells, poliovirus replicon assay The Journal of cell biology Medium 36305789
2023 Phosphorylation of specific conserved N-terminal residues of GBF1 (S233, S371, Y377, Y515) differentially regulates its role in cytokinesis versus Golgi homeostasis/secretion. Phosphomimetic GBF1 mutants (and S233A) are fully capable of maintaining Golgi architecture and supporting secretion, but cause multi-nucleation and inhibit progression through cytokinetic bridge resolution, revealing distinct phosphorylation-regulated interaction networks for GBF1 in different cellular processes. Phosphomimetic/phosphodeficient site-directed mutagenesis, Golgi homeostasis assay, cargo trafficking assay, cytokinesis assay (multi-nucleation), cell-cycle analysis Scientific reports Medium 37604968
2024 AMPK associates with the Golgi and its activation by pharmacological activators leads to Golgi fragmentation via GBF1 phosphorylation at Thr1337. Golgi disassembly upon AMPK activation is blocked in cells expressing a non-phosphorylatable GBF1-T1337A mutant (generated by gene editing). AMPK activation also delays trafficking of a plasma membrane-targeted protein through the Golgi complex. AMPK-α subunit gene knockouts, CRISPR gene editing (GBF1-T1337A knock-in), pharmacological AMPK activators, Golgi fragmentation quantification, cargo trafficking assay Journal of cell science High 39575556
2024 Enterovirus 3A proteins (from EV-A71, CVB3, poliovirus, EV-D68) interact with GBF1 via N-terminal-conserved 3A residues, sequestering GBF1 and inhibiting ARF1 activation. This induces severe ER stress/UPR and apoptosis via the PERK/CHOP pathway. Pharmaceutical inhibition of PERK suppresses cell death caused by enterovirus infection. ER expansion and accumulation of ER-resident proteins were observed in infected cells. 3A expression constructs, co-immunoprecipitation, ARF1 activation assay, ER morphology analysis by imaging, UPR/PERK/CHOP pathway markers (Western blot), PERK inhibitor treatment, cell viability assay Journal of virology Medium 38904364
2024 GBF1 deficiency in human lens epithelium cells activates XBP1s in the unfolded protein response (UPR) signaling pathway and enhances autophagy in an mTOR-independent manner. A heterozygous GBF1 mutation (T1287I) reduces GBF1 protein levels in human lens epithelium cells. Heterozygous Gbf1 knockout mice display a cataract phenotype. Genetic analysis, siRNA/shRNA knockdown in human lens epithelium cell line, Western blot for UPR markers (XBP1s), autophagy assay, Gbf1 heterozygous knockout mouse Human genetics Medium 39110251
2025 Substrate stiffness stimulates conventional secretion through a Src-FAK-AMPK-GBF1 signaling axis. Phosphoproteomic analysis identified GBF1 as a mechano-responsive regulator. GBF1 phosphorylation state orchestrates post-Golgi cargo sorting, directing proteins toward secretion versus lysosomal degradation. AMPK acts as a stiffness-dependent upstream regulator of GBF1 phosphorylation. Substrate stiffness manipulation, phosphoproteomic analysis, Src/FAK inhibition, AMPK activation/inhibition, secretion assays, lysosomal degradation assays bioRxivpreprint Low

Source papers

Stage 0 corpus · 79 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2011 Chlamydia trachomatis co-opts GBF1 and CERT to acquire host sphingomyelin for distinct roles during intracellular development. PLoS pathogens 191 21909260
2004 Dynamics of GBF1, a Brefeldin A-sensitive Arf1 exchange factor at the Golgi. Molecular biology of the cell 188 15616190
1999 GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5. The Journal of cell biology 172 10402461
2009 GBF1, a guanine nucleotide exchange factor for Arf, is crucial for coxsackievirus B3 RNA replication. Journal of virology 153 19740986
2008 Mouse hepatitis coronavirus RNA replication depends on GBF1-mediated ARF1 activation. PLoS pathogens 130 18551169
2006 A viral protein that blocks Arf1-mediated COP-I assembly by inhibiting the guanine nucleotide exchange factor GBF1. Developmental cell 130 16890159
2007 Rab1b interacts with GBF1 and modulates both ARF1 dynamics and COPI association. Molecular biology of the cell 115 17429068
2009 Identification of GBF1 as a cellular factor required for hepatitis C virus RNA replication. Journal of virology 107 19906930
2008 Unfolded protein response and cell death after depletion of brefeldin A-inhibited guanine nucleotide-exchange protein GBF1. Proceedings of the National Academy of Sciences of the United States of America 89 18287014
2007 Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking. Journal of cell science 89 17956946
2006 GBF1, a cis-Golgi and VTCs-localized ARF-GEF, is implicated in ER-to-Golgi protein traffic. Journal of cell science 89 16926190
2007 Distinct functions for Arf guanine nucleotide exchange factors at the Golgi complex: GBF1 and BIGs are required for assembly and maintenance of the Golgi stack and trans-Golgi network, respectively. Molecular biology of the cell 86 18003980
2006 Effects of picornavirus 3A Proteins on Protein Transport and GBF1-dependent COP-I recruitment. Journal of virology 83 17005635
2008 Characterization of class I and II ADP-ribosylation factors (Arfs) in live cells: GDP-bound class II Arfs associate with the ER-Golgi intermediate compartment independently of GBF1. Molecular biology of the cell 74 18524849
2005 Dissection of membrane dynamics of the ARF-guanine nucleotide exchange factor GBF1. Traffic (Copenhagen, Denmark) 70 15813748
2013 Targeting of the Arf-GEF GBF1 to lipid droplets and Golgi membranes. Journal of cell science 68 23943872
2003 The membrane-tethering protein p115 interacts with GBF1, an ARF guanine-nucleotide-exchange factor. EMBO reports 68 12634853
2015 Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets. Traffic (Copenhagen, Denmark) 67 26031340
2013 The Sec7 guanine nucleotide exchange factor GBF1 regulates membrane recruitment of BIG1 and BIG2 guanine nucleotide exchange factors to the trans-Golgi network (TGN). The Journal of biological chemistry 66 23386609
2013 Recruitment of PI4KIIIβ to coxsackievirus B3 replication organelles is independent of ACBD3, GBF1, and Arf1. Journal of virology 65 24352456
2012 ARF1 and GBF1 generate a PI4P-enriched environment supportive of hepatitis C virus replication. PloS one 61 22359663
2009 Analysis of endocytic pathways in Drosophila cells reveals a conserved role for GBF1 in internalization via GEECs. PloS one 61 19707569
2007 Molecular determinants of the interaction between coxsackievirus protein 3A and guanine nucleotide exchange factor GBF1. Journal of virology 61 17329336
2010 Poliovirus replication requires the N-terminus but not the catalytic Sec7 domain of ArfGEF GBF1. Cellular microbiology 57 20497182
2011 Interaction between the triglyceride lipase ATGL and the Arf1 activator GBF1. PloS one 54 21789191
2013 AMPK phosphorylates GBF1 for mitotic Golgi disassembly. Journal of cell science 50 23418352
2010 The phosphatidylinositol 4-kinase PI4KIIIalpha is required for the recruitment of GBF1 to Golgi membranes. Journal of cell science 49 20530568
2017 GBF1 and Arf1 function in vesicular trafficking, lipid homoeostasis and organelle dynamics. Biology of the cell 46 28985001
2014 Quantitative proteomic analysis of host-virus interactions reveals a role for Golgi brefeldin A resistance factor 1 (GBF1) in dengue infection. Molecular & cellular proteomics : MCP 46 24855065
2007 Interactions between conserved domains within homodimers in the BIG1, BIG2, and GBF1 Arf guanine nucleotide exchange factors. The Journal of biological chemistry 43 17640864
2010 Differential effects of the putative GBF1 inhibitors Golgicide A and AG1478 on enterovirus replication. Journal of virology 42 20504936
2012 GBF1 bears a novel phosphatidylinositol-phosphate binding module, BP3K, to link PI3Kγ activity with Arf1 activation involved in GPCR-mediated neutrophil chemotaxis and superoxide production. Molecular biology of the cell 40 22573891
2019 A GBF1-Dependent Mechanism for Environmentally Responsive Regulation of ER-Golgi Transport. Developmental cell 37 31056345
2010 LG186: An inhibitor of GBF1 function that causes Golgi disassembly in human and canine cells. Traffic (Copenhagen, Denmark) 37 20854417
2010 Phosphorylation and membrane dissociation of the ARF exchange factor GBF1 in mitosis. The Biochemical journal 34 20175751
2012 GBF1 (Gartenzwerg)-dependent secretion is required for Drosophila tubulogenesis. Journal of cell science 33 22302994
2007 The Arf GEF GBF1 is required for GGA recruitment to Golgi membranes. Traffic (Copenhagen, Denmark) 30 17666033
2018 GBF1 and Arf1 interact with Miro and regulate mitochondrial positioning within cells. Scientific reports 26 30459446
2017 Identification of GBF1 as a cellular factor required for hepatitis E virus RNA replication. Cellular microbiology 26 29112323
2019 BioID Performed on Golgi Enriched Fractions Identify C10orf76 as a GBF1 Binding Protein Essential for Golgi Maintenance and Secretion. Molecular & cellular proteomics : MCP 23 31519766
2017 CSFV proliferation is associated with GBF1 and Rab2. Journal of biosciences 23 28229964
2017 The Arf GEF GBF1 and Arf4 synergize with the sensory receptor cargo, rhodopsin, to regulate ciliary membrane trafficking. Journal of cell science 23 29025970
2018 Investigation of the role of GBF1 in the replication of positive-sense single-stranded RNA viruses. The Journal of general virology 20 29923822
1998 Human GBF1 is a ubiquitously expressed gene of the sec7 domain family mapping to 10q24. Genomics 20 9828135
2016 Impairment of Cargo Transportation Caused by gbf1 Mutation Disrupts Vascular Integrity and Causes Hemorrhage in Zebrafish Embryos. The Journal of biological chemistry 18 28003365
2015 Oligomerization of the Sec7 domain Arf guanine nucleotide exchange factor GBF1 is dispensable for Golgi localization and function but regulates degradation. American journal of physiology. Cell physiology 18 26718629
2019 The Guanine Nucleotide Exchange Factor GBF1 Participates in Rotavirus Replication. Journal of virology 17 31270230
2015 Phosphorylation Affects DNA-Binding of the Senescence-Regulating bZIP Transcription Factor GBF1. Plants (Basel, Switzerland) 17 27135347
2013 The ArfGEF GBF-1 Is Required for ER Structure, Secretion and Endocytic Transport in C. elegans. PloS one 17 23840591
2018 Inheritance of the Golgi Apparatus and Cytokinesis Are Controlled by Degradation of GBF1. Cell reports 16 29898406
2020 SNPs in SNCA, MCCC1, DLG2, GBF1 and MBNL2 are associated with Parkinson's disease in southern Chinese population. Journal of cellular and molecular medicine 15 32652860
2020 De Novo and Inherited Variants in GBF1 are Associated with Axonal Neuropathy Caused by Golgi Fragmentation. American journal of human genetics 15 32937143
2019 Functional and Physical Interaction between the Arf Activator GBF1 and Hepatitis C Virus NS3 Protein. Journal of virology 14 30567983
2019 Quantitative Proteomics of Uukuniemi Virus-host Cell Interactions Reveals GBF1 as Proviral Host Factor for Phleboviruses. Molecular & cellular proteomics : MCP 14 31570497
2020 Regulating the regulators: role of phosphorylation in modulating the function of the GBF1/BIG family of Sec7 ARF-GEFs. FEBS letters 13 32333796
2020 Role of the Guanine Nucleotide Exchange Factor GBF1 in the Replication of RNA Viruses. Viruses 13 32599855
2019 A Redundant Mechanism of Recruitment Underlies the Remarkable Plasticity of the Requirement of Poliovirus Replication for the Cellular ArfGEF GBF1. Journal of virology 13 31375590
2018 Highly conserved motifs within the large Sec7 ARF guanine nucleotide exchange factor GBF1 target it to the Golgi and are critical for GBF1 activity. American journal of physiology. Cell physiology 13 29443553
2003 Characterization of alternatively spliced and truncated forms of the Arf guanine nucleotide exchange factor GBF1 defines regions important for activity. Biochemical and biophysical research communications 13 12646181
2021 Src activates retrograde membrane traffic through phosphorylation of GBF1. eLife 12 34870592
2021 Rab1b-GBF1-ARF1 Secretory Pathway Axis Is Required for Birnavirus Replication. Journal of virology 11 34878889
2020 Rab1b-GBF1-ARFs mediated intracellular trafficking is required for classical swine fever virus replication in swine umbilical vein endothelial cells. Veterinary microbiology 9 32605744
2024 Enterovirus 3A protein disrupts endoplasmic reticulum homeostasis through interaction with GBF1. Journal of virology 8 38904364
2022 Viral protein engagement of GBF1 induces host cell vulnerability through synthetic lethality. The Journal of cell biology 8 36305789
2018 The Arf-GDP-regulated recruitment of GBF1 to Golgi membranes requires domains HDS1 and HDS2 and a Golgi-localized protein receptor. Journal of cell science 8 29507113
2022 ARF1 with Sec7 Domain-Dependent GBF1 Activates Coatomer Protein I To Support Classical Swine Fever Virus Entry. Journal of virology 6 35044210
2021 Loss of Arf Guanine Nucleotide Exchange Factor GBF1 Activity Disturbs Organelle Dynamics in Mouse Oocytes. Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada 5 33478608
2019 Rab18 regulates lipolysis via Arf/GBF1 and adipose triglyceride lipase. Biochemical and biophysical research communications 4 31610914
2024 AMPK associates with and causes fragmentation of the Golgi by phosphorylating the guanine nucleotide exchange factor GBF1. Journal of cell science 3 39575556
2020 Viral protein engagement of GBF1 induces host cell vulnerability through synthetic lethality. bioRxiv : the preprint server for biology 3 33173868
2022 AG1478 Elicits a Novel Anti-Influenza Function via an EGFR-Independent, GBF1-Dependent Pathway. International journal of molecular sciences 2 35628375
2023 Site-specific phosphorylations of the Arf activator GBF1 differentially regulate GBF1 function in Golgi homeostasis and secretion versus cytokinesis. Scientific reports 1 37604968
2026 Broad-spectrum antiviral activity of antisense oligonucleotides targeting GBF1 against SARS-CoV-2 and influenza viruses. iScience 0 41743235
2026 Intracellular protein GBF1 displays significant associations with amyloid pathology in Alzheimer's disease. Alzheimer's & dementia : the journal of the Alzheimer's Association 0 41988936
2024 GBF1 deficiency causes cataracts in human and mouse. Human genetics 0 39110251
2024 A Novel GBF1 Variant in a Charcot-Marie-Tooth Type 2: Insights from Familial Analysis. Genes 0 39766823
2020 A miRNA screen procedure identifies garz as an essential factor in adult glia functions and validates Drosophila as a beneficial 3Rs model to study glial functions and GBF1 biology. F1000Research 0 32595956
2016 Correction: Phosphorylation Affects DNA-Binding of the Senescence-Regulating bZIP Transcription Factor GBF1. Plants 2015, 4, 691-709. Plants (Basel, Switzerland) 0 27598219
2005 Development of monoclonal antibodies against GBF1 and their use in studying its functions. Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research 0 16318580

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