Affinage

ARFGAP1

ADP-ribosylation factor GTPase-activating protein 1 · UniProt Q8N6T3

Length
406 aa
Mass
44.7 kDa
Annotated
2026-06-09
42 papers in source corpus 29 papers cited in narrative 29 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

ARFGAP1 is a GTPase-activating protein for Arf1 that times GTP hydrolysis during COPI vesicle biogenesis by sensing membrane curvature, thereby coupling the Arf1 GTPase cycle to the geometry of the budding vesicle (PMID:14654841, PMID:19927117). Curvature sensing is achieved through two ALPS (ArfGAP1 Lipid Packing Sensor) motifs that are unstructured in solution but fold into amphipathic helices when inserting hydrophobic residues into loosely packed lipids of highly curved membranes; ALPS1 couples GAP activity to curvature and ALPS2 reinforces membrane binding and Golgi targeting (PMID:15944734, PMID:17253781, PMID:19927117). Unlike the coatomer-dependent ArfGAP2/3, ARFGAP1 binds membranes directly in a curvature-dependent manner, and its Golgi recruitment additionally depends on a hydrophobic stretch around Leu207/Trp211 and on phosphatidic acid generated by PLD2 (PMID:16316994, PMID:19015319, PMID:25354038). Within the COPI system ARFGAP1 functions intimately with the coat: it binds dilysine cargo motifs, promotes coatomer binding to cargo and coatomer polymerization, and undergoes coatomer- and Arf1-dependent cytosol/Golgi exchange, while cargo proteins such as p24β1 suppress its GAP activity to license vesicle formation (PMID:12379802, PMID:11748249, PMID:15795316, PMID:22279613). Through distinct C-terminal tryptophan-based motifs ARFGAP1 engages clathrin adaptors and coatomer separately, allowing it to participate in both COPI transport and AP-2-dependent endocytosis (PMID:20211604, PMID:21499258). Beyond Arf1, ARFGAP1 acts as a GAP toward Arl1 at the TGN to control retrograde transport and toward ARF6 during endocytosis of membrane transporters, and it restrains actin reorganization by inhibiting Rac1 activation (PMID:33715220, PMID:34040545, PMID:21483700). ARFGAP1 also intersects Parkinson's disease biology: it is a GAP for LRRK2 that enhances LRRK2 GTP hydrolysis and modulates LRRK2 kinase activity and neurotoxicity, and reciprocally it is a substrate of LRRK2, whose phosphorylation of the ALPS2 motif (Ser284/Thr291/Thr292) redirects ARFGAP1 from Golgi to cytoplasm and modulates Golgi vesicle formation and neurite outgrowth (PMID:22363216, PMID:22423108, PMID:42094986). Additional roles include inhibition of mTORC1 lysosomal recruitment via its ALPS motifs under amino-acid deprivation (PMID:33988249).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 2002 High

    Established whether ARFGAP1 acts merely as an uncoating enzyme or as an integral part of the COPI machinery, by showing it is present stoichiometrically and binds cargo directly.

    Evidence Reconstituted COPI vesicle formation from Golgi membranes with purified components plus dilysine-cargo binding assays

    PMID:12379802

    Open questions at the time
    • Stoichiometry of ARFGAP1 on vesicles later disputed
    • Did not resolve curvature dependence of GAP timing
  2. 2001 High

    Answered how cargo loading is coordinated with the Arf1 GTPase timer, showing the p24β1 cytoplasmic domain binds ARFGAP1 and inhibits its GAP activity.

    Evidence Synthetic peptide binding and in vitro GTP hydrolysis assays on liposomes and Golgi membranes

    PMID:11748249

    Open questions at the time
    • Whether other cargo classes regulate GAP activity similarly
    • In vivo significance of inhibition during budding
  3. 2003 High

    Resolved why GTP hydrolysis is timed to vesicle budding, demonstrating that ARFGAP1 catalytic activity is dramatically stimulated as bilayer curvature increases.

    Evidence Time-resolved in vitro GTP hydrolysis and COPI disassembly assays on size-controlled liposomes

    PMID:14654841

    Open questions at the time
    • Did not yet identify the structural sensor of curvature
  4. 2005 High

    Identified the molecular curvature sensor as the ALPS motif and showed Golgi localization depends on specific hydrophobic residues, while live-cell FRAP linked ARFGAP1 dynamics to coatomer and Arf1.

    Evidence Mutagenesis, CD, limited proteolysis, liposome binding, GFP localization, and FRAP in living cells

    PMID:15657398 PMID:15795316 PMID:15944734 PMID:16316994

    Open questions at the time
    • Number of curvature-sensing motifs not yet established
    • How ALPS folding is regulated in vivo unknown
  5. 2007 High

    Demonstrated ARFGAP1 carries a second ALPS motif (ALPS2) that strongly reinforces curvature-dependent membrane binding and Golgi targeting.

    Evidence Quantitative liposome binding, CD, and GFP localization with mutagenesis

    PMID:17253781

    Open questions at the time
    • Functional division of labor between ALPS1 and ALPS2 in vivo
    • Regulation of ALPS2 not addressed
  6. 2008 High

    Distinguished ARFGAP1 from paralogs by showing it binds membranes directly in a curvature-dependent manner rather than via coatomer, and linked it to neuronal cargo (GAT-1).

    Evidence Comparative membrane-binding and GAP assays with purified ArfGAP1/2/3; co-IP and siRNA with axonal targeting readout

    PMID:19015319 PMID:19020038

    Open questions at the time
    • Mechanism of GAT-1 sorting by ARFGAP1 incomplete
    • Generality of cargo handling
  7. 2009 High

    Provided spatial proof of curvature-restricted activity, showing ALPS motifs bind only positively curved tubes and generate an Arf1 activity gradient.

    Evidence Membrane tube pulling with optical tweezers and molecular motors plus fluorescence microscopy

    PMID:19927117

    Open questions at the time
    • Whether such gradients form on native Golgi
    • Coupling to coat assembly in cells
  8. 2009 Medium

    Challenged the stoichiometric-coat model by showing catalytic amounts of ARFGAP1 reduce COPI vesicle yield, favoring an uncoating role.

    Evidence Defined reconstitution with titrated ArfGAP1 and vesicle quantification

    PMID:19055691

    Open questions at the time
    • Directly contradicts other reconstitution studies
    • Single-lab result not independently reconciled
  9. 2011 High

    Mapped how ARFGAP1 engages two coat systems through separate C-terminal motifs, enabling roles in both COPI transport and AP-2-dependent endocytosis, and clarified its action on coatomer polymerization.

    Evidence GST pulldowns, peptide competition, co-IP, selective disruption mutants and transport/EM assays

    PMID:20211604 PMID:21499258 PMID:22279613

    Open questions at the time
    • How dual coat engagement is temporally segregated
    • Whether AP-1 vs AP-2 binding is regulated
  10. 2012 High

    Established a reciprocal enzymatic relationship with the Parkinson's kinase LRRK2 — ARFGAP1 as a GAP for LRRK2 and a substrate that modulates LRRK2 toxicity.

    Evidence In vitro GTPase and kinase assays, co-IP in cells and brain, siRNA/dominant-negative and Drosophila toxicity readouts

    PMID:22363216 PMID:22423108

    Open questions at the time
    • Phosphosites on ARFGAP1 not yet mapped
    • Physiological context of LRRK2 regulation
  11. 2014 Medium

    Extended ARFGAP1 function to lipid droplet biology, viral hijacking, and PLD2-dependent Golgi recruitment.

    Evidence Microscopy, fractionation, co-IP, siRNA, PI4P measurement, and PLD2 inhibition/depletion

    PMID:24623438 PMID:25354038 PMID:25397679

    Open questions at the time
    • Mechanism of lipid droplet association unclear
    • Single-lab observations for each role
  12. 2017 Medium

    Placed ARFGAP1 in actin-cytoskeleton control downstream of Arf1/PLD1, restraining Rac1 and limiting bacterial entry.

    Evidence siRNA, actin imaging, Rac1 activation assays and pathogen entry assays with epistasis

    PMID:21483700 PMID:29141986

    Open questions at the time
    • Direct molecular target in Rac1 inhibition not defined
    • Whether catalytic vs non-catalytic domain mediates each effect
  13. 2021 Medium

    Broadened the GAP repertoire to Arl1 at the TGN and ARF6 in endocytosis, and revealed ALPS-dependent inhibition of mTORC1 lysosomal recruitment under amino-acid deprivation.

    Evidence In vitro GTPase/activity assays, GFP-Arl1 and EAAT3 endocytosis assays, co-IP, lysosomal fractionation and ALPS mutants

    PMID:33715220 PMID:33988249 PMID:34040545

    Open questions at the time
    • How substrate selection among Arf1/Arl1/ARF6 is achieved
    • Mechanism of mTORC1 inhibition single-lab
  14. 2026 Medium

    Defined the LRRK2 phosphorylation sites on the ALPS2 motif and showed phosphorylation redirects ARFGAP1 from Golgi to cytoplasm, altering vesicle formation and neurotoxicity.

    Evidence In vitro kinase assays with site-directed mutagenesis, phospho-mimetic/null mutants, localization, interactome and primary neuron morphology

    PMID:42094986

    Open questions at the time
    • In vivo confirmation of phosphoregulation
    • Functional meaning of VDAC interaction
    • Single-lab and very recent

Open questions

Synthesis pass · forward-looking unresolved questions
  • How ARFGAP1's many context-specific roles — COPI/AP coat cycling, Arl1/ARF6 GAP activity, mTORC1, actin, and LRRK2 crosstalk — are integrated and regulated within a single cell remains unresolved.
  • Unified model of substrate/pathway selection lacking
  • Stoichiometric-coat versus uncoating controversy unsettled
  • Physiological relevance of LRRK2 phosphoregulation in vivo unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 5 GO:0008289 lipid binding 4 GO:0060090 molecular adaptor activity 3 GO:0140096 catalytic activity, acting on a protein 3
Localization
GO:0005794 Golgi apparatus 4 GO:0031410 cytoplasmic vesicle 3 GO:0005829 cytosol 2 GO:0005811 lipid droplet 1
Pathway
R-HSA-1643685 Disease 5 R-HSA-5653656 Vesicle-mediated transport 5 R-HSA-9609507 Protein localization 3
Partners
AP-1AP-2ARF1ARF6ARL1COPB1LRRK2TMED2
Complex memberships
COPI coat

Evidence

Reading pass · 29 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2003 ArfGAP1-catalyzed GTP hydrolysis in Arf1 and COPI coat disassembly are stimulated over two orders of magnitude as membrane bilayer curvature increases toward that of a transport vesicle, establishing a mechanistic coupling between lipid packing/curvature and the timing of GTP hydrolysis during COPI vesicle budding. Time-resolved in vitro GTP hydrolysis and COPI disassembly assays on liposomes of controlled size Nature High 14654841
2005 A central ~40-amino-acid ALPS (ArfGAP1 Lipid Packing Sensor) motif in ArfGAP1 is unstructured in solution but folds into an amphipathic helix upon inserting bulky hydrophobic residues between loosely packed lipids on highly curved membranes, and this motif is necessary for coupling ArfGAP1 GAP activity to membrane curvature. Site-directed mutagenesis, limited proteolysis, circular dichroism, liposome-binding assays The EMBO journal High 15944734
2002 ARFGAP1 promotes COPI vesicle formation and cargo sorting by functioning as a stoichiometric component of the COPI coat; it binds directly to dilysine motifs of cargo proteins, and its presence at levels comparable to coatomer on reconstituted vesicles supports a coat function rather than purely an uncoating function. Reconstituted COPI vesicle formation from Golgi membranes with purified components; direct binding assays between GAP and dilysine cargo motifs The Journal of cell biology High 12379802
2001 The cytoplasmic domain of p24β1 cargo protein binds directly to ArfGAP1 and inhibits ArfGAP1-mediated GTP hydrolysis on Arf1 bound to liposomes and Golgi membranes, providing a mechanism whereby cargo suppresses GAP activity during vesicle formation. Synthetic peptide binding assays; in vitro GTP hydrolysis assays on liposomes and Golgi membranes The Journal of cell biology High 11748249
2005 ArfGAP1 catalytic activity is required for COPI vesicle formation from Golgi membranes, and ARF1 (not ARFGAP1) plays a key direct role in binding SNARE cargo proteins; ArfGAP1 promotes coatomer binding to cargo proteins. In vitro COPI vesicle reconstitution from Golgi membranes; cargo-binding assays with purified components The Journal of cell biology High 15657398
2005 FRAP analysis in living cells shows that ArfGAP1 undergoes fast cytosol/Golgi exchange, with ~40% of exchange dependent on engagement with coatomer and Arf1; permanent Arf1 activation traps ArfGAP1 on Golgi in a coatomer-dependent manner, demonstrating interdependent roles in the COPI coat assembly-disassembly cycle in vivo. FRAP of GFP-tagged ArfGAP1, Arf1, and coatomer in living cells; pharmacological Arf1 activation The Journal of cell biology High 15795316
2007 ArfGAP1 contains a second lipid-packing sensor motif (ALPS2) that also forms an amphipathic helix at the surface of small vesicles; ALPS2 reinforces membrane interaction ~40-fold relative to ALPS1 alone and contributes to Golgi localization of ArfGAP1 in vivo. Quantitative liposome-binding assays; circular dichroism; GFP localization in cells; mutagenesis Biochemistry High 17253781
2005 Golgi localization of ArfGAP1 depends on hydrophobic residues (including Leu-207 and Trp-211) within a short stretch (residues 204–214); alanine substitution of these residues strongly diminishes Golgi localization and reduces in vitro GAP activity on Golgi-bound Arf1. Site-directed mutagenesis; GFP-fusion localization; in vitro GAP activity assay on Golgi membranes The Journal of biological chemistry High 16316994
2008 Unlike ArfGAP2 and ArfGAP3 (which require coatomer for membrane recruitment), ArfGAP1 binds membranes directly in a curvature-dependent manner, demonstrating that ArfGAP1 is a membrane curvature-dependent ArfGAP with a distinct recruitment mechanism from the coatomer-dependent ArfGAPs. Membrane-binding assays with purified proteins; in vitro GAP activity assays in the presence/absence of coatomer The Journal of cell biology High 19015319
2008 Catalytic amounts of ArfGAP1 significantly reduce the yield of purified COPI vesicles in a defined reconstitution assay, suggesting ArfGAP1 acts as an uncoating factor rather than a stoichiometric coat component under these conditions; Arf1 (not ArfGAP1) constitutes a stoichiometric component of the COPI coat. Defined reconstitution assay for COPI vesicle formation from Golgi membranes with titrated ArfGAP1; COPI vesicle purification and quantification Traffic Medium 19055691
2009 ArfGAP1 ALPS motifs bind exclusively to membrane tubes (positively curved membranes, radius threshold ~35 nm) and not to flat giant vesicle membranes; mixing catalytic amounts of ArfGAP1 with Arf1-GTP on tube-connected vesicles generates a smooth Arf1 gradient along the tube, demonstrating spatial regulation of Arf1 activity by membrane curvature sensing. Membrane tube pulling from giant vesicles using molecular motors and optical tweezers; fluorescence microscopy of labeled proteins The EMBO journal High 19927117
2005 ArfGAP1-induced GTP hydrolysis disassembles AP-1 adaptor oligomers from membranes; AP-1 stimulates ArfGAP1 activity in a reciprocal interaction, suggesting a role for AP-1 in regulating the Arf1 GTPase timer. In vitro reconstitution with purified AP-1, Arf1, liposomes, and ArfGAP1; gel filtration/sedimentation to detect oligomers Molecular biology of the cell Medium 16093346
2010 ArfGAP1 interacts with coat proteins through tryptophan-based motifs in its C-terminal region: a (329)WETF sequence binds clathrin adaptors AP-1 and AP-2, while the extreme C-terminal motif (405)AADEGWDNQNW is required for coatomer binding via the δ-subunit of the coatomer adaptor-like subcomplex. GST pulldown with peptides; mutagenesis; peptide competition; reporter fusion assay in vivo Biochemical and biophysical research communications Medium 20211604
2011 Distinct regions of ARFGAP1 separately interact with AP-2 and coatomer; selectively disrupting the ARFGAP1–AP-2 interaction inhibits AP-2-dependent endocytosis, while disrupting ARFGAP1–coatomer interaction inhibits COPI transport, showing ARFGAP1 participates in both pathways through independent coat-binding regions. Co-immunoprecipitation; dominant-negative and deletion mutant analysis; transport assays Nature cell biology High 21499258
2008 ARFGAP1 binds directly to the C-terminus of GAT-1 (GABA transporter-1), and surface expression of a COPII-independent GAT-1 mutant (GAT1-RL/AS) requires ARFGAP1; correct axonal targeting of GAT-1 requires COPII-dependent ER export and is lost for the ARFGAP1-dependent bypass mutant. Co-immunoprecipitation/pull-down; siRNA knockdown; immunofluorescence in neuronal cells The Journal of neuroscience Medium 19020038
2012 ArfGAP1 acts as a GTPase-activating protein for LRRK2, markedly enhancing LRRK2 GTP hydrolysis activity; ArfGAP1 also promotes LRRK2 kinase activity; reciprocally, LRRK2 directly phosphorylates ArfGAP1 in vitro; silencing ArfGAP1 rescues G2019S LRRK2-induced neurite shortening in primary cortical neurons. Co-immunoprecipitation in mammalian cells and brain lysates; in vitro GTPase assay; in vitro kinase assay; siRNA knockdown with neurite morphology readout PLoS genetics High 22363216
2012 ArfGAP1 is the first identified GAP for LRRK2, binding predominantly via the WD40 and kinase domains of LRRK2; ArfGAP1 increases LRRK2 GTPase activity and regulates LRRK2 toxicity in vitro and in Drosophila; LRRK2 inhibits ArfGAP1 GAP activity while ArfGAP1 reduces LRRK2 autophosphorylation and kinase activity; Δ64-ArfGAP1 (dominant-negative) and shRNA knockdown of ArfGAP1 reduce LRRK2 toxicity. In vitro GTPase assay; in vitro kinase assay; co-immunoprecipitation; dominant-negative expression; Drosophila in vivo toxicity assay; shRNA knockdown The Journal of neuroscience High 22423108
2011 ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization: ArfGAP1 increases coatomer-induced LUV deformation and, with cargo peptides, supports self-assembly of coatomer into spherical structures in the absence of membranes; ArfGAP1 overexpression in vivo induces vesicle accumulation while allowing normal COPI cargo trafficking. Electron microscopy of LUV deformation; coatomer self-assembly assay; in vivo overexpression with trafficking assay Cellular logistics Medium 22279613
2011 The non-catalytic C-terminal domain of ARFGAP1 (residues sufficient in GAP273 truncation) regulates actin cytoskeleton reorganization by inhibiting Rac1 activation upstream of Rac1; overexpression of constitutively active Rac1 or ARF6 suppresses the actin/spreading defects caused by this domain. Overexpression of truncation mutants; live-cell imaging; Rac1 activation assays; epistasis with constitutively active GTPases PloS one Medium 21483700
2014 HCV NS5A interacts with ARFGAP1 via a conserved cluster of positively charged amino acids in NS5A; this interaction hijacks ARFGAP1 to remove the PI4P phosphatase Sac1 (a COPI cargo) from the HCV replication site, thereby maintaining high PI4P levels required for HCV RNA replication. Co-immunoprecipitation; mutational analysis of NS5A; siRNA knockdown of ARFGAP1; PI4P level measurement; HCV replication assay Journal of virology Medium 24623438
2014 ARFGAP1 associates transiently with lipid droplets upon oleate addition in hepatocytes; cAMP addition shifts ARFGAP1 from lipid droplets to the Golgi; overexpression and knockdown of ARFGAP1 affect lipid droplet formation. Fluorescence microscopy; subcellular fractionation; overexpression and siRNA knockdown with lipid droplet quantification PloS one Medium 25397679
2021 ArfGAP1 interacts with mTORC1 in the absence of amino acids and inhibits mTORC1 lysosomal localization and activation; the ALPS motifs of ArfGAP1 are required for this interaction and regulation of mTORC1 activity. Co-immunoprecipitation; lysosomal fractionation; mTORC1 activity assays; ALPS motif mutants; amino acid stimulation/deprivation The EMBO journal Medium 33988249
2021 ArfGAP1 directly interacts with GTP-bound Arl1 and exhibits GAP activity toward Arl1 in vitro; ArfGAP1 overexpression (but not GAP activity-deficient mutant) causes dissociation of Arl1 from the TGN; ArfGAP1 knockdown impairs endosome-to-TGN retrograde transport of Shiga toxin B-subunit, similar to constitutively active Arl1. In vitro GTPase assay; activity pull-down; GFP-Arl1 localization; Shiga toxin trafficking assay; siRNA knockdown FASEB journal Medium 33715220
2021 ARFGAP1 promotes constitutive endocytosis of the glutamate transporter EAAT3 via its GAP activity using ARF6 as the substrate; a single phenylalanine residue (F508) in the EAAT3 C-terminus is required for ARFGAP1-promoted AP-2-dependent endocytosis; ARFGAP1 was identified as an EAAT3-interacting protein by mass spectrometry. Mass spectrometry; co-immunoprecipitation; GAP activity-deficient mutants; endocytosis assays; mutagenesis of F508 Frontiers in physiology Medium 34040545
2017 ArfGAP1 controls actin cytoskeleton reorganization downstream of Arf1 and phospholipase D1 (PLD1) via the M3 muscarinic receptor pathway, restricting Mycobacterium tuberculosis entry into epithelial cells; ArfGAP1 silencing leads to uncontrolled actin reorganization and increased Mtb uptake, while infection by Shigella flexneri and Yersinia pseudotuberculosis is unaffected. siRNA knockdown; actin imaging; bacterial entry assays with multiple pathogens; genetic pathway analysis EMBO reports Medium 29141986
2014 Phosphatidic acid generated by phospholipase D2 (PLD2) is required for ArfGAP1 recruitment to Golgi membranes; inhibition or depletion of PLD2 prevents ArfGAP1 Golgi localization. PLD2 inhibition and siRNA depletion; fluorescence microscopy of ArfGAP1 localization PloS one Medium 25354038
2026 LRRK2 phosphorylates ArfGAP1 within its ALPS2 motif at residues Ser284, Thr291, and Thr292 in vitro; phospho-mimicking mutations at these sites impair ArfGAP1 Golgi localization, redirect it to the cytoplasm, increase its interaction with mitochondrial VDAC proteins, block Golgi-derived vesicle formation after ER stress, and impair neurite outgrowth inhibition; phospho-null mutations protect against G2019S LRRK2 neurotoxicity. In vitro kinase assay with site-directed mutagenesis; phospho-null and phospho-mimetic mutant analysis; subcellular localization; interactome analysis; primary neuron morphology assay Frontiers in molecular neuroscience Medium 42094986
2023 In Drosophila border cells, ArfGAP1 is required to maintain receptor tyrosine kinases (guidance receptors) at the plasma membrane; loss of ArfGAP1 increases receptor levels in late endosomes, increases late endosome/lysosome number and size, reduces directional chemotaxis, and genetic interactions suggest ArfGAP1 acts on Lrrk to regulate receptor sorting. Drosophila genetics; fluorescence imaging of receptor localization; endosome/lysosome quantification; genetic interaction analysis iScience Medium 37599820
2025 ATG2A localizes to extra-Golgi ARFGAP1-positive puncta during autophagosome biogenesis; ARFGAP1 itself is dispensable for macroautophagy but marks membranes that associate with the autophagic machinery; when autophagosome formation or early secretory pathway is perturbed, ARFGAP1 and Rab1a accumulate at ectopic sites with autophagic components. Proximity labeling (BioID); fluorescence microscopy; siRNA depletion; co-immunoprecipitation bioRxivpreprint Low 40196537

Source papers

Stage 0 corpus · 42 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif. The EMBO journal 316 15944734
2003 Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature. Nature 261 14654841
2002 ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat. The Journal of cell biology 161 12379802
2001 Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: a role for ArfGAP1. The Journal of cell biology 147 11748249
2012 GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1. PLoS genetics 112 22363216
2005 ARFGAP1 plays a central role in coupling COPI cargo sorting with vesicle formation. The Journal of cell biology 110 15657398
2007 Two lipid-packing sensor motifs contribute to the sensitivity of ArfGAP1 to membrane curvature. Biochemistry 100 17253781
2012 ArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2. The Journal of neuroscience : the official journal of the Society for Neuroscience 90 22423108
2005 ArfGAP1 dynamics and its role in COPI coat assembly on Golgi membranes of living cells. The Journal of cell biology 74 15795316
2009 ArfGAP1 generates an Arf1 gradient on continuous lipid membranes displaying flat and curved regions. The EMBO journal 62 19927117
2008 Differential roles of ArfGAP1, ArfGAP2, and ArfGAP3 in COPI trafficking. The Journal of cell biology 61 19015319
2008 ArfGAP1 activity and COPI vesicle biogenesis. Traffic (Copenhagen, Denmark) 43 19055691
2011 ARFGAP1 promotes AP-2-dependent endocytosis. Nature cell biology 39 21499258
2014 Hepatitis C virus NS5A hijacks ARFGAP1 to maintain a phosphatidylinositol 4-phosphate-enriched microenvironment. Journal of virology 34 24623438
2021 ArfGAP1 inhibits mTORC1 lysosomal localization and activation. The EMBO journal 30 33988249
2008 Sec24- and ARFGAP1-dependent trafficking of GABA transporter-1 is a prerequisite for correct axonal targeting. The Journal of neuroscience : the official journal of the Society for Neuroscience 30 19020038
2005 Oligomerization and dissociation of AP-1 adaptors are regulated by cargo signals and by ArfGAP1-induced GTP hydrolysis. Molecular biology of the cell 24 16093346
2005 Golgi localization determinants in ArfGAP1 and in new tissue-specific ArfGAP1 isoforms. The Journal of biological chemistry 22 16316994
2012 ArfGAP1 function in COPI mediated membrane traffic: currently debated models and comparison to other coat-binding ArfGAPs. Histology and histopathology 21 22806901
2017 ArfGAP1 restricts Mycobacterium tuberculosis entry by controlling the actin cytoskeleton. EMBO reports 20 29141986
2010 ArfGAP1 interacts with coat proteins through tryptophan-based motifs. Biochemical and biophysical research communications 18 20211604
2011 ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization. Cellular logistics 17 22279613
2008 Topology of amphipathic motifs mediating Golgi localization in ArfGAP1 and its splice isoforms. The Journal of biological chemistry 17 18195007
2013 Involvement of small ArfGAP1 (SMAP1), a novel Arf6-specific GTPase-activating protein, in microsatellite instability oncogenesis. Oncogene 15 23752192
2011 GAPs: Terminator versus effector functions and the role(s) of ArfGAP1 in vesicle biogenesis. Cellular logistics 15 21686252
2014 ARFGAP1 is dynamically associated with lipid droplets in hepatocytes. PloS one 14 25397679
2021 ARFGAP1 binds to classical swine fever virus NS5A protein and enhances CSFV replication in PK-15 cells. Veterinary microbiology 11 33721634
2021 Glutamine Regulates Cell Growth and Casein Synthesis through the CYTHs/ARFGAP1-Arf1-mTORC1 Pathway in Bovine Mammary Epithelial Cells. Journal of agricultural and food chemistry 11 34096300
2021 BPIFB3 interacts with ARFGAP1 and TMED9 to regulate non-canonical autophagy and RNA virus infection. Journal of cell science 10 33277377
2021 ArfGAP1 acts as a GTPase-activating protein for human ADP-ribosylation factor-like 1 protein. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 8 33715220
2021 Constitutive Endocytosis of the Neuronal Glutamate Transporter Excitatory Amino Acid Transporter-3 Requires ARFGAP1. Frontiers in physiology 8 34040545
2015 Identification of Atg2 and ArfGAP1 as Candidate Genetic Modifiers of the Eye Pigmentation Phenotype of Adaptor Protein-3 (AP-3) Mutants in Drosophila melanogaster. PloS one 8 26565960
2011 The non-catalytic carboxyl-terminal domain of ARFGAP1 regulates actin cytoskeleton reorganization by antagonizing the activation of Rac1. PloS one 8 21483700
2014 Phospholipase D2 is involved in the formation of Golgi tubules and ArfGAP1 recruitment. PloS one 6 25354038
2017 High abundance of ArfGAP1 found in the mossy fibers in hilus of the dentate gyrus region of the mouse brain. PloS one 4 29240824
2018 Detecting phospholipase activity with the amphipathic lipid packing sensor motif of ArfGAP1. Biochemical and biophysical research communications 2 30249399
2025 ATG2A engages Rab1a and ARFGAP1 positive membranes during autophagosome biogenesis. bioRxiv : the preprint server for biology 1 40196537
2023 C9orf72 Toxic Species Affect ArfGAP-1 Function. Cells 1 37566088
2023 ArfGAP1 regulates the endosomal sorting of guidance receptors to promote directed collective cell migration in vivo. iScience 1 37599820
2026 LRRK2 regulates ArfGAP1 membrane localization, activity and neuronal toxicity via phosphorylation within its lipid-sensing ALPS2 motif. bioRxiv : the preprint server for biology 0 41648595
2026 LRRK2 regulates ArfGAP1 membrane localization, activity and neuronal integrity via phosphorylation within its lipid-sensing ALPS2 motif. Frontiers in molecular neuroscience 0 42094986
2025 ARFGAP1 serves as a critical host factor during E30 infection: QS11 inhibits viral pathogenesis in hFcRn-IFNAR-/- mice. Virology journal 0 41163005

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