| 1991 |
RAB1B is required for vesicular transport from the ER to the cis-Golgi compartment and between successive cis- and medial-Golgi compartments, as demonstrated by reconstitution of ER-to-Golgi transport in a cell-free assay and immunolocalization of RAB1B to both ER and Golgi compartments. |
Cell-free reconstitution assay of ER-to-Golgi transport; monoclonal antibody inhibition; subcellular fractionation and immunolocalization |
The Journal of Cell Biology |
High |
1918138
|
| 1989 |
RAB1B protein binds GTP and GDP specifically and possesses intrinsic GTPase activity; the Lys21→Met mutant abolishes GTP binding, while the Ala65→Thr mutant reduces GTPase activity and retains autophosphorylation competence in the presence of GTP. |
In vitro biochemical assay with purified recombinant protein; site-directed mutagenesis; GTP/GDP binding and GTPase activity measurements |
FEBS Letters |
High |
2509243
|
| 1993 |
The effector domain of RAB1B (residues I41, D44) is essential for geranylgeranylation by GGTase II; mutations I41N and D44N in the effector domain essentially abolish isoprenylation, while mutations in the N-terminal variable region, β3 strand, or Loop 7 do not reduce isoprenylation. |
In vitro isoprenylation assay using reticulocyte lysates; site-directed mutagenesis; deletion analysis |
The Journal of Biological Chemistry |
High |
8325834
|
| 1995 |
RAB1B is required for ER-to-Golgi transport of beta-amyloid precursor protein (βAPP); dominant-negative RAB1B mutants (N121I, S22N) block conversion of immature Endo-H-sensitive βAPP to mature O-glycosylated form and inhibit secretion of APP-α and Aβ peptide. |
Co-expression of dominant-negative RAB1B mutants with βAPP in 293 cells; [35S]methionine pulse-chase; Endo-H sensitivity assay; immunoprecipitation |
The Journal of Biological Chemistry |
High |
7738040
|
| 1995 |
Dominant-negative RAB1B (N121I) blocks ER-to-Golgi transport and maturation of the LDL receptor, preventing its conversion from the Endo-H-sensitive 120-125 kDa form to the mature 160-170 kDa form and preventing its delivery to the cell surface. |
Co-expression of dominant-negative RAB1B with LDL receptor in 293 cells; [35S]methionine pulse-chase; Endo-H sensitivity; sulfo-NHS-biotin cell surface labeling |
Journal of Receptor and Signal Transduction Research |
Medium |
8673720
|
| 1996 |
Association of geranylgeranylated RAB1B with GDP-dissociation inhibitors (GDI-α and GDI-2) is required for recycling of prenylated RAB1B to the cytosol but not for initial membrane targeting; the effector-domain mutant D44N fails to form GDI complexes yet is still delivered to intracellular membranes. |
Co-immunoprecipitation with anti-FLAG beads; in vitro GDI binding assay; [3H]mevalonate metabolic labeling; subcellular fractionation; immunofluorescence |
The Journal of Biological Chemistry |
High |
8631911
|
| 1996 |
RAB1B geranylgeranylation by Rab-GGTase preferentially requires the GDP-bound conformation of the substrate in cell-free assays; the GTPase-deficient Q67L mutant is poorly prenylated when GTP predominates but prenylated normally when GDP is the predominant nucleotide. |
Cell-free geranylgeranylation assay with defined nucleotide compositions; [3H]mevalonate metabolic labeling in transfected 293 cells; co-IP with GDI |
The Biochemical Journal |
Medium |
8836150
|
| 1998 |
The Switch 2 domain (α2 helix, residues I73, Y78, A81) of RAB1B is essential for binding to Rab escort protein (REP); mutations in this helix prevent prenylation by preventing association of nascent RAB1B with REP, while REP binds preferentially to GDP-bound RAB1B. |
Cell-free geranylgeranylation assay; [3H]mevalonate metabolic labeling; [32P]orthophosphate nucleotide binding assay; gel filtration co-fractionation of REP-RAB1B complexes from transfected 293 cells |
Molecular Biology of the Cell |
High |
9437002
|
| 1999 |
Correct intracellular localization and tight membrane association of RAB1B depends on GDP/GTP exchange; inactive (S22N, N121I) and constitutively active (Q67L) mutants are not tightly integrated into target membranes in BHK cells. |
Expression of RAB1B mutants in BHK cells; subcellular localization by immunofluorescence; membrane association assay; co-expression with Mss4 |
International Journal of Oncology |
Medium |
10493955
|
| 2001 |
RAB1B interacts specifically with the Golgi matrix protein GM130 in a GTP-dependent manner, requiring the hypervariable regions of the N- and C-termini of RAB1B; the RAB1B binding site on GM130 is distinct from the p115 and Grasp65 binding sites. |
Yeast two-hybrid screen; in vitro binding assays; deletion and mutagenesis mapping |
EMBO Reports |
Medium |
11306556
|
| 2003 |
Inactive RAB1B (N121I mutant) blocks ER-to-Golgi transport and induces Golgi disruption by compromising COPI recruitment (release of β-COP into cytosol); this phenotype can be rescued by expressing ARF1 or its GEF GBF1, placing RAB1B upstream of ARF1/GBF1-mediated COPI recruitment. The active Q67L mutant confers resistance to BFA-induced Golgi disruption. |
Expression of RAB1B dominant-negative and constitutively active mutants in cells; immunofluorescence; subcellular fractionation for β-COP; BFA treatment; co-expression rescue experiments |
Molecular Biology of the Cell |
High |
12802079
|
| 2007 |
Active RAB1B (Q67L) increases GBF1 and COPI association at ER exit sites and stabilizes ARF1 on Golgi membranes; GBF1 is identified as a RAB1B effector via its N-terminal domain; RAB1B siRNA reduces GBF1 membrane association; FRAP shows rapid RAB1B cycling at the Golgi (t½ ~120 s) with minimal microtubule dependence. |
Dominant mutant expression; co-immunoprecipitation; siRNA knockdown; live-cell time-lapse microscopy; FRAP |
Molecular Biology of the Cell |
High |
17429068
|
| 2010 |
The Legionella effector DrrA AMPylates RAB1B at Tyr77 (switch II region), covalently attaching AMP; this modification restricts GTPase-activating protein access, rendering RAB1B constitutively active. DrrA also acts as a guanine nucleotide exchange factor for RAB1B. |
Biochemical AMPylation assay with purified proteins; mass spectrometry identification of modification site; GEF activity assay; GAP accessibility assay |
Science |
High |
20651120
|
| 2010 |
RAB1B is required for ER-to-Golgi transport of Ebolavirus matrix protein VP40, and dominant-negative RAB1B interferes with VP40-mediated particle formation; this occurs through the RAB1B→GBF1→ARF1→COPI pathway. |
Dominant-negative RAB1B expression; VP40 particle formation assay; GBF1 and ARF1 inhibition studies |
Journal of Virology |
Medium |
20164217
|
| 2010 |
RAB1B interacts with COPII components Sec23, Sec24, and Sec31 and modulates COPII assembly/disassembly kinetics at ER exit sites; RAB1B inhibition (by dominant-negative or siRNA) changes COPII phenotype and delays cargo sorting at ER exit sites, as measured by FRAP. |
Co-immunoprecipitation; siRNA knockdown; dominant-negative mutant expression; FRAP at ER exit sites; cargo transport assay |
European Journal of Cell Biology |
Medium |
21093099
|
| 2012 |
MTMR6 (phosphatidylinositol 3-phosphatase) preferentially interacts with GDP-bound RAB1B via its GRAM domain and partially colocalizes with RAB1B in pericentrosomal and peri-Golgi regions; RAB1B regulates the localization of MTMR6, and MTMR6 reduction accelerates VSV-G transport (a RAB1B-dependent process); both RAB1B and MTMR6 are required for omegasome tubule formation in autophagy. |
Co-immunoprecipitation with GDP/GTP-locked RAB1B mutants; siRNA knockdown of RAB1B and MTMR6; immunofluorescence colocalization; VSV-G transport assay; DFCP1-induced omegasome assay |
The Journal of Biological Chemistry |
Medium |
23188820
|
| 2013 |
Legionella LepB inactivates RAB1B by acting as a GTPase-activating protein (GAP) via an atypical RabGAP mechanism reminiscent of classical GAPs (distinct from mammalian TBC-like GAPs); the crystal structure of the RAB1B:LepB complex reveals an unusual fold in the GAP domain. |
Crystal structure determination of RAB1B:LepB complex; biochemical GAP activity assays; mutagenesis |
EMBO Reports |
High |
23288104
|
| 2014 |
The vesicle docking protein p115 enhances RAB1B activation and membrane association: p115 binds RAB1B through its cc2 domain, p115 inhibition causes RAB1B dissociation from Golgi membranes, and constitutively active RAB1B suppresses the COPI recruitment defect caused by p115 inhibition, establishing p115 as a functional upstream activator of RAB1B in COPI recruitment. |
siRNA knockdown of p115; dominant-active RAB1B rescue experiments; co-immunoprecipitation domain mapping; immunofluorescence for COPI and RAB1B localization |
Cellular Logistics |
Medium |
25332841
|
| 2015 |
Loss of RAB1B leads to elevated TGF-β receptor 1 (TβR1) levels through decreased ubiquitin-dependent degradation, increased phospho-SMAD3, and TGF-β-induced EMT, revealing that RAB1B acts upstream of TGF-β/SMAD signaling as a metastasis suppressor. |
siRNA knockdown and overexpression of RAB1B in TNBC cell lines; Western blotting for TβR1, pSMAD3; ubiquitination assay; in vitro migration/invasion assays; in vivo xenograft |
Oncotarget |
Medium |
25970785
|
| 2015 |
Host RAB1B is recruited to the Yersinia-containing vacuole (YCV) and is required for Y. pestis evasion of phagosome maturation; RAB1B knockdown prevents YCV acidification inhibition and alters LAMP1 association with the YCV, demonstrating RAB1B recruitment is a mechanism by which Y. pestis subverts phagosomal killing. |
siRNA/shRNA knockdown of RAB1B in macrophages; immunofluorescence for RAB1B on YCV; phagosomal pH measurement; LAMP1 colocalization assay; bacterial survival assay |
PLoS Pathogens |
Medium |
26495854
|
| 2016 |
PITPNC1 promotes malignant secretion by binding Golgi-resident PI4P and localizing RAB1B to the Golgi; RAB1B localization to the Golgi recruits GOLPH3, which facilitates Golgi extension and enhanced vesicular release of pro-invasive factors. |
Biochemical PI4P binding assay; RAB1B localization by immunofluorescence; GOLPH3 co-immunoprecipitation; vesicular release assay; siRNA knockdown |
Cancer Cell |
Medium |
26977884
|
| 2016 |
Adenylylation of Tyr77 of RAB1B by DrrA stabilizes the active (GTP-like) conformation independently of bound nucleotide, primarily through electrostatic effects of the additional negative charge in the switch II region; Phe45-adenine stacking has only minor influence. |
Molecular dynamics simulation; advanced sampling simulations |
Scientific Reports |
Low |
26818796
|
| 2016 |
RAB1B dynamically associates with ER exit sites, VTCs, and the Golgi complex; RAB1B dwell time at ER exit sites is regulated by GBF1, and RAB1B membrane cycling kinetics at ERES are dependent on GBF1 membrane association and activity, as shown by live-cell dual-expression imaging and BFA washout experiments. |
Live-cell dual-color fluorescence microscopy; FRAP; brefeldin A washout cargo-sorting assay; GBF1 dominant-negative and siRNA experiments |
PLoS One |
Medium |
27500526
|
| 2017 |
RAB1B is associated with ATG9A-containing vesicles in mammalian cells; RAB1B knockdown suppresses autophagy and causes ATG9A accumulation at intermediate membrane structures at autophagosome formation sites, demonstrating RAB1B is required for proper ATG9A vesicle dynamics during autophagosome formation. |
Immunoisolation of ATG9A vesicles followed by proteomics; siRNA knockdown of RAB1B; fluorescence microscopy of ATG9A and autophagy markers; autophagy flux assay |
FASEB Journal |
Medium |
28522593
|
| 2017 |
Staphylococcus aureus alpha-hemolysin induces formation of dynamic tubular structures (Saf) labeled with RAB1B, RAB7, and LC3; these tubules emerge from the S. aureus-containing phagosome and their formation depends on RAB1B activity, microtubule integrity, Kinesin-1, and RILP. |
Live-cell imaging; dominant-negative RAB1B expression; microtubule disruption; siRNA knockdown of kinesin/RILP; fluorescence microscopy |
Frontiers in Cellular and Infection Microbiology |
Medium |
29046869
|
| 2018 |
RAB1B is a direct transcriptional target of RUNX1; RUNX1 binds the RAB1B promoter at consensus RUNX1 sites (shown by ChIP and EMSA); RUNX1 knockdown impairs ER-to-Golgi vesicle trafficking and Golgi structure in megakaryocytic cells, and these defects are rescued by RAB1B reconstitution; RAB1B is required for trafficking of von Willebrand factor to α-granules. |
Chromatin immunoprecipitation; EMSA; luciferase promoter assay with RUNX1 site mutations; siRNA knockdown of RUNX1 and RAB1B; RAB1B rescue experiments; ER-to-Golgi transport assay; vWF trafficking assay |
Blood Advances |
High |
29632235
|
| 2019 |
RAB1B promotes antiviral innate immune signaling by forming a protein complex with TRAF3 and facilitating the interaction between TRAF3 and MAVS, thereby enhancing RIG-I pathway activation and IFN-β induction; RAB1B deletion dampens IFN-β signaling and increases Zika virus susceptibility. |
Co-immunoprecipitation; RAB1B overexpression and CRISPR deletion in multiple human cell types; IFN-β luciferase reporter assay; viral infection assay (Zika virus) |
The Journal of Biological Chemistry |
Medium |
31375559
|
| 2019 |
RAB1B directly binds FMDV IRES RNA and stimulates IRES-mediated translation; IRES-driven RNA localizes in close proximity to RAB1B at the ER-Golgi interface, while dominant-negative RAB1B that disorganizes the Golgi abolishes this colocalization. |
Proteomics-based IRES interactor identification; direct RNA binding assay; IRES translation assay; RNA-FISH imaging with RAB1B colocalization |
Life Science Alliance |
Medium |
30655362
|
| 2020 |
Human GOLPH3 is a bona fide effector of RAB1B; GOLPH3 interacts directly with RAB1B in a nucleotide-dependent manner favoring the GTP-locked active state; expression of GTP-locked RAB1B variants reduces GOLPH3 distribution at the Golgi apparatus. |
Co-immunoprecipitation with GTP/GDP-locked RAB1B mutants; direct binding assay; immunofluorescence for GOLPH3 localization |
PLoS One |
Medium |
32790781
|
| 2023 |
The Legionella enzyme Lem3 acts as a dephosphocholinase on RAB1B, hydrolytically removing the phosphocholine moiety added by AnkX at Ser76; the crystal structures of Lem3 alone and in complex with RAB1B reveal that Lem3 acts by locally unfolding RAB1B at the switch II region and that Lem3 shares structural similarity with metal-dependent protein phosphatases. |
Crystal structure determination of Lem3 apo and Lem3:RAB1B complex (covalent capture); enzymatic dephosphocholination assay; structural analysis |
Nature Communications |
High |
37076474
|
| 2024 |
RAB1B promotes DGAT2 redistribution from the ER to the lipid droplet surface (shown by FRET between DGAT2 and RAB1B activity mutants), thereby facilitating lipid droplet growth; TBC1D20 (the RAB1B GAP mutated in Warburg Micro syndrome) loss-of-function alters LD metabolism and DGAT2 redistribution consistently with elevated RAB1B activity. |
FRET between DGAT2 and RAB1B activity mutants; dominant-negative RAB1B overexpression to block LD formation; TBC1D20 mutant fibroblasts from WARBM model mice; fluorescence microscopy |
Science Advances |
Medium |
38809969
|
| 2025 |
TBC1D22B is a GAP that directly targets RAB1B; TBC1D22B overexpression inhibits ER-to-Golgi transport in a GAP-activity-dependent manner, and RAB1B silencing phenocopies TBC1D22B-induced trafficking defects, placing RAB1B as the direct substrate of TBC1D22B in ER-to-Golgi transport regulation. |
Proximity-labeling and co-immunoprecipitation proteomics; RUSH system ER-to-Golgi transport assay; RAB1B siRNA knockdown; GAP-dead mutant rescue experiments |
Advanced Science |
Medium |
40878439
|