| 1991 |
Rab3A associates with synaptic vesicle membranes at the cell periphery (not at the Golgi), and undergoes translocation to the cell surface during massive exocytosis, suggesting it is part of a regulatory machinery assembled onto vesicles in preparation for exocytosis. |
Immunofluorescence, subcellular fractionation, live imaging of frog motor end plates |
The Journal of cell biology |
High |
1655810
|
| 1990 |
Rab3A is associated with chromaffin granule membranes in adrenal medulla chromaffin cells; it is partially cytosolic and partially membrane-bound, and membrane association requires hydrophobic modification (likely fatty acid acylation or lipid anchor), consistent with a role in regulated secretion. |
Subcellular fractionation, immunoadsorption with anti-dopamine beta-hydroxylase antibody, detergent/salt extraction |
Proceedings of the National Academy of Sciences of the United States of America |
High |
2165599
|
| 1991 |
Rab3A membrane attachment to synaptic vesicles is mediated by posttranslational polyisoprenylation (geranylgeranylation) of its C-terminal Cys-X-Cys sequence; this modification is required for membrane binding and is distinct from intracellular targeting to synaptic vesicles. |
Compactin inhibition (mevalonate-dependent), mutagenesis of C-terminal cysteines, biochemical fractionation |
Neuron |
High |
1648935
|
| 1992 |
Rab3A effector domain peptides stimulate exocytotic fusion (degranulation) in mast cells in a Mg2+- and ATP-dependent, sequence-specific manner, suggesting activated Rab3A causes exocytotic fusion via an effector protein at the target membrane. |
Patch-clamp capacitance measurements, intracellular perfusion of synthetic peptides in mast cells |
Nature |
High |
1331813
|
| 1992 |
A target protein for GTP-bound Rab3A (smg p25A) of ~85-86 kDa exists in bovine brain membranes; cross-linking is GTP-dependent and specific to Rab3A over other small GTPases, identifying the first putative Rab3A effector (later characterized as rabphilin-3A). |
Chemical cross-linking (disuccinimidyl suberate), SDS-PAGE, protein purification from brain membranes |
The Journal of biological chemistry |
High |
1597436
|
| 1992 |
Rab3A effector domain peptide (rab3AL) stimulates amylase release from permeabilized pancreatic acini in an ATP-dependent manner, potentiates GTPγS-induced secretion, and lowers the Ca2+ threshold for secretion, demonstrating a role for Rab3-like proteins in a distal step of regulated secretion. |
Streptolysin-O permeabilized pancreatic acinar cells, amylase release assay |
Proceedings of the National Academy of Sciences of the United States of America |
High |
1371881
|
| 1992 |
The geranylgeranyl moiety, but not the carboxymethyl moiety, of Rab3A is essential for interactions with membranes and with the GDP dissociation inhibitor (GDI); unmodified recombinant Rab3A lacks both activities. |
In vitro geranylgeranylation assay with purified geranylgeranyltransferase, membrane-binding assay, GDI sensitivity assay |
The Journal of biological chemistry |
High |
1315770
|
| 1993 |
Rabphilin-3A is a GTP-dependent effector of Rab3A: it forms a complex specifically with GTPγS-bound (not GDP-bound) Rab3A, contains two C2 domains homologous to synaptotagmin, and its N-terminal domain binds Rab3A while its C-terminal C2 domains bind Ca2+/phospholipid. |
cDNA cloning, pulldown/complex formation assay, domain deletion analysis with recombinant fragments |
Molecular and cellular biology |
High |
8384302
|
| 1993 |
The N-terminal domain of rabphilin-3A binds GTP-Rab3A and inhibits Rab3A-GAP-stimulated GTPase activity, thereby prolonging the GTP-bound active state of Rab3A; the C-terminal C2 domain does not bind Rab3A but mediates Ca2+/phospholipid binding. |
Recombinant fragment domain analysis, GTPase activity assay, GAP inhibition assay |
The Journal of biological chemistry |
High |
8226731 8262955
|
| 1991 |
Rab3A has a detergent-soluble, brain-membrane-associated GAP activity that accelerates its GTPase; the GAP activity is thermolabile, trypsin-sensitive, and behaves as an integral membrane protein; a cytosolic GAP activity is also present. |
GTPase activity assay, membrane/cytosol fractionation, gel filtration chromatography |
The Journal of biological chemistry |
High |
1847129
|
| 1993 |
The effector domain (residues 51-59) of Rab3A is required for interaction with Rab3A-GRF (guanine nucleotide releasing factor) and for cross-linking to the putative target protein p85; mutations in this domain abolish GRF sensitivity and most interactions, while the first G-domain has modest effects. |
Site-directed mutagenesis, GRF activity assay, GAP activity assay, cross-linking |
The Journal of biological chemistry |
High |
8226229 8387493
|
| 1993 |
Rab3A GTPase cycle is regulated by GDP dissociation inhibitor (GDI), guanine nucleotide releasing factor (GRF), and GAP; in PC12 cells, cytosolic Rab3A is predominantly GDP-bound, while membrane-associated Rab3A is ~50% GTP-bound; GDI acts only on GDP-Rab3A and antagonizes GRF but not GAP. |
Nucleotide binding assay, GDI/GRF/GAP activity assays in PC12 cell fractions |
The Journal of biological chemistry |
High |
8226729
|
| 1994 |
Rab geranylgeranyltransferase, together with Rab escort protein, catalyzes geranylgeranylation of both adjacent C-terminal cysteines of Rab3A (Cys-Ala-Cys-Cys motif), as established by mass spectrometric analysis of in vitro prenylated proteins. |
In vitro prenylation assay with purified enzyme, tryptic peptide HPLC, electrospray mass spectrometry |
Proceedings of the National Academy of Sciences of the United States of America |
High |
7991565
|
| 1994 |
Rab3A plays a role in the recruitment of synaptic vesicles for exocytosis during repetitive stimulation but is not essential for basal exocytosis; rab3A-null mice show increased synaptic depression after short trains of stimuli and 70% reduction in rabphilin levels at synapses. |
Homologous recombination knockout, electrophysiological recordings in hippocampal CA1 cells, protein quantitation by immunoblot |
Nature |
High |
7911226
|
| 1994 |
Synaptic targeting of rabphilin-3A depends on Rab3A (and Rab3C); in rab3A-deficient mice, rabphilin-3A is decreased in synapses of neurons primarily expressing rab3A and accumulates in perikarya; rabphilin-3A binds Rab3C in vitro, explaining rescue in neurons expressing Rab3C. |
Rab3A knockout mice analysis, immunocytochemistry, in vitro binding assay |
Neuron |
High |
7946335
|
| 1994 |
Rab3A overexpression or expression of a constitutively GTP-bound mutant (Q81L) inhibits Ca2+-dependent exocytosis in chromaffin cells; this inhibition acts as a 'prefusion block', suggesting Rab3A may be an inhibitor of secretion that is overcome by elevated Ca2+. |
Transient transfection of chromaffin cells, human growth hormone reporter assay for exocytosis, Ca2+-stimulated secretion from permeabilized cells |
The Journal of biological chemistry |
High |
8144603
|
| 1994 |
GTP cleavage by synaptic vesicle-bound Rab3A occurs during exocytosis: membrane-associated Rab3A is predominantly GTP-bound at rest, while cytosolic Rab3A is GDP-bound; alpha-latrotoxin-induced exocytosis causes a significant increase in GDP/GTP ratio of Rab3A. |
Nucleotide binding analysis of synaptosome fractions, alpha-latrotoxin stimulation, GDP/GTP ratio measurement |
The Journal of biological chemistry |
High |
7929154
|
| 1994 |
Rab3A effector domain peptides specifically stimulate insulin exocytosis in electroporated beta-cells and interact with a cytosolic protein doublet (REEP-1 and REEP-2) via photocrosslinking; these proteins are membrane-associated under basal conditions and released to cytosol upon exocytosis stimulation. |
Electroporation of beta-cells, insulin release assay, 125I-radiolabeled photoactivatable crosslinking peptide |
The Journal of biological chemistry |
Medium |
7961732
|
| 1994 |
Rabphilin-3A is phosphorylated by cAMP-dependent protein kinase (PKA) at its N-terminal region (approximately 0.8 mol phosphate per mol protein); Rab3A itself is not a PKA substrate. |
In vitro phosphorylation assay with purified PKA and recombinant proteins |
Biochemical and biophysical research communications |
High |
7945346
|
| 1995 |
Rabphilin-3A overexpression enhances regulated secretion in chromaffin cells (~30%), while antisense inhibition reduces it; C2 domain deletion mutants strongly inhibit exocytosis despite retaining the Rab3A-binding domain, indicating the C2 domains are required for rabphilin-3A's positive regulatory function downstream of Rab3A interaction. |
cDNA transfection in chromaffin cells, growth hormone reporter assay, permeabilized cell secretion assay |
The Journal of biological chemistry |
High |
7622481
|
| 1995 |
The Cys-rich zinc-finger domain of rabphilin-3A binds two Zn2+ ions and is necessary but not sufficient for Rab3A binding; a minimal Rab3A-binding domain spans residues 45-170; Rab3A targeting to vesicles is independent of its interaction with rabphilin-3A (Rab3A T54A mislocalizes from rabphilin but not from vesicles). |
Domain deletion/mutagenesis, GFP-fusion localization in PC12 cells, metal binding assay |
Molecular and cellular biology |
High |
8756657
|
| 1995 |
Rabin3 (a novel 50-kDa brain protein) interacts specifically with Rab3A and Rab3D via the Rab3A effector domain; multiple effector domain mutations abolish the interaction; Rabin3 has sequence similarity to yeast Sec2p (a GEF for Sec4p, the Rab3A yeast ortholog), suggesting a conserved GEF-like role. |
Yeast two-hybrid screen, effector domain mutagenesis, GST pulldown |
Molecular and cellular biology |
Medium |
7532276
|
| 1997 |
Ca2+/calmodulin causes Rab3A to dissociate from synaptic membranes in vitro by forming a 1:1 complex with Rab3A that requires both the lipidated C terminus and bound guanine nucleotide; this differs from GDI in being Ca2+-dependent and less stringently requiring GDP. |
In vitro membrane dissociation assay, complex formation assay, synthetic peptide competition |
The Journal of biological chemistry |
High |
9252412
|
| 1997 |
Rab3A acts at a late step in synaptic vesicle fusion (after docking): rab3A-null mice have a normal readily releasable pool size but altered Ca2+-triggered fusion, with more exocytic events occurring within a brief time window after nerve impulse arrival. |
Electrophysiological analysis of rab3A-deficient mice, analysis of readily releasable pool, quantal analysis |
Nature |
High |
9194562
|
| 1997 |
Rab3A is essential for mossy fiber LTP in the hippocampus; rab3A-null mice show abolishment of LTP at hippocampal mossy fiber synapses while short-term plasticities remain normal, placing Rab3A as a required presynaptic component of this NMDA-independent form of LTP. |
Rab3A knockout mice, hippocampal slice electrophysiology, LTP induction protocols |
Nature |
High |
9252190
|
| 1998 |
In mossy fiber synapses, cAMP enhances glutamate release by multiple mechanisms including direct activation of the secretory apparatus (Ca2+ sensitivity), and only this last mechanism requires Rab3A; forskolin still enhances KCl- and sucrose-induced release in rab3A-deficient synaptosomes but fails to enhance ionomycin-induced release. |
CA3 synaptosome preparations from rab3A-null mice, glutamate release assay with multiple stimuli |
Neuron |
High |
9856469
|
| 1999 |
Crystal structure of activated Rab3A/GTP/Mg2+ bound to the effector domain of rabphilin-3A (2.6 Å resolution) reveals two interfaces: one involving Rab3A switch I and switch II regions (nucleotide-state sensitive), and a second involving a unique deep pocket (RabCDR) that interacts with the SGAWFF element of rabphilin-3A and determines effector specificity. |
X-ray crystallography at 2.6 Å |
Cell |
High |
10025402
|
| 1999 |
Rab3A is associated with the acrosomal membrane in rat sperm; synthetic Rab3 effector domain peptide inhibits ionophore-triggered acrosomal exocytosis in a concentration-dependent manner, suggesting Rab3A acts as an inhibitory regulator of the acrosome reaction. |
Immunogold EM, sucrose gradient fractionation, acrosome reaction assay with effector peptide |
Developmental biology |
Medium |
10373312
|
| 2000 |
GTP-bound Rab3A triggers acrosomal exocytosis in permeabilized human spermatozoa; GDP-bound Rab3A and Rab11-GTP are inactive; recombinant GDI inhibits GTPγS-stimulated exocytosis, indicating Rab3A (or a Rab3 isoform) is a required positive regulator of acrosomal exocytosis. |
Streptolysin-O permeabilized sperm, recombinant Rab3A loaded with GTP/GDP, acrosome reaction assay |
Biology of reproduction |
High |
10727281
|
| 2000 |
Calcium-dependent acrosomal exocytosis requires both active Rab3A (GTP-bound) and NSF; Rab3A activation protects NSF from NEM inhibition and prevents exchange of endogenous NSF with dominant-negative NSF mutants; Rab3A and NSF act in a coordinated cascade for acrosome fusion. |
Permeabilized sperm exocytosis assay, NEM inhibition, dominant-negative NSF protein microinjection |
Proceedings of the National Academy of Sciences of the United States of America |
High |
10954749
|
| 2001 |
GRAB is a physiological GEF for Rab3A: it directly catalyzes GDP/GTP exchange on Rab3A, interacts with InsP6K1, and regulates depolarization-induced dopamine and growth hormone release from neuroendocrine cells. |
Protein cloning, GEF activity assay, dopamine release assay in PC12 cells, chromaffin cell secretion assay |
Neuron |
High |
11516400
|
| 2001 |
Rab3A is required for activity-dependent recruitment of synaptic vesicles to and docking at the active zone: rab3A deletion completely abolishes depolarization-induced vesicle accumulation near active zones without affecting resting vesicle number or single-stimulus secretion; replenishment of docked vesicles after exhaustive stimulation is also impaired. |
Electron microscopy of nerve terminals from rab3A-null mice, vesicle distribution quantitation, secretion assay |
Molecular biology of the cell |
High |
11598194
|
| 2003 |
Rim1 interacts with Rab3A/B/C/D and other Rabs; Rim2 interacts with Rab3A/B/C/D and Rab8A; an acidic cluster (Glu-50, Glu-51, Glu-52) in the first alpha-helical region of Rim2's Rab-binding domain is a critical determinant of Rab3A recognition, as shown by mutagenesis and chimeric analysis. |
Cotransfection assay with 42 Rab proteins, site-directed mutagenesis, chimeric protein analysis |
The Journal of biological chemistry |
High |
12578829
|
| 2003 |
Rabconnectin-3 consists of alpha and beta subunits; the beta subunit directly binds Rab3 GEP (the GEF for Rab3A), while the alpha subunit indirectly associates with Rab3 GAP, forming a complex that coordinates Rab3A GTPase cycle regulation at synaptic vesicles. |
Co-immunoprecipitation from synaptic vesicle fractions, cDNA cloning, direct binding assay |
Genes to cells |
Medium |
12786944
|
| 2003 |
Rab3A null mice develop fasting hyperglycemia and ablated first-phase insulin release in vivo; isolated Rab3A-null islets show ~60-70% reduction in secretagogue-induced insulin release with normal glucose oxidation and Ca2+ flux, placing Rab3A function downstream of Ca2+ signaling at the level of secretory granule transport/exocytosis. |
Rab3A knockout mice, glucose tolerance test, isolated islet insulin release, glucose oxidation and Ca2+ flux assays |
The Journal of biological chemistry |
High |
12510060
|
| 2004 |
Synapsin I is a Rab3A effector on synaptic vesicles: it stimulates GTP binding and GTPase activity of Rab3A; conversely, Rab3A inhibits synapsin I binding to F-actin and actin bundling; synapsin I prevents RabGDI-induced Rab3A dissociation from vesicles; Rab3A levels on vesicles are reduced in synapsin KO mice. |
In vitro GTPase/GTP binding assay, F-actin binding/bundling assay, RabGDI dissociation assay, synapsin KO mice |
The Journal of biological chemistry |
High |
15265868
|
| 2005 |
Zn7-metallothionein-3 binds reversibly to Rab3A in its GDP-bound form (Kd = 2.6 µM) but not to GTP-Rab3A; the interaction site maps to the effector binding region; GDP exchange kinetics are unaffected by the interaction, indicating Zn7MT-3 is not a GEF but may regulate Rab3A via its effector domain. |
Affinity precipitation, surface plasmon resonance, Rab3A mutagenesis, GDP exchange kinetics assay |
Biochemistry |
High |
15736926
|
| 2006 |
Rab3A and Rab27A cooperatively regulate the docking step of dense-core vesicles to the plasma membrane in PC12 cells: siRNA silencing of either reduces docked vesicle number without altering exocytotic kinetics; simultaneous silencing causes a significantly greater decrease in docking. |
siRNA knockdown, TIRF microscopy single-cell analysis in PC12 cells |
Journal of cell science |
High |
16684812
|
| 2006 |
Active zone recruitment of Munc13-1 and ubMunc13-2 requires binding to RIM1α; a single point mutation (I121N) in Munc13s abolishes RIM1α (Rab3A-interacting molecule) binding and prevents synaptic recruitment of Munc13s; Munc13-1 levels and active zone enrichment are reduced in RIM1α-deficient brain. |
Point mutagenesis, co-IP, RIM1α KO mice immunostaining and Western blot |
The Journal of biological chemistry |
High |
16704978
|
| 2007 |
FRAP analysis shows EGFP-Rab3A exchanges rapidly between granules and cytosol (faster recovery than Rab27A or granule cargo ppANF), consistent with a GTP hydrolysis-dependent cycle; newly synthesized secretory granules preferentially recruit Rab3A and Rab27A, suggesting these Rabs mark young granules for preferential exocytosis. |
FRAP in PC12 cells, post-transfection time-course of granule association, live cell imaging during stimulation |
Journal of cell science |
High |
17311845
|
| 2007 |
Rab3A cycling between GTP and GDP forms (not either locked state alone) is required for its docking function; both GTP- and GDP-locked Rab3A mutants fail to promote vesicle docking; furthermore, the docking function of Rab3A requires Munc18-1, as wild-type Rab3A cannot promote docking in munc18-1 null chromaffin cells. |
Expression of Rab3A mutants in wild-type and munc18-1 null chromaffin cells, electron microscopy vesicle distribution |
PloS one |
High |
17637832
|
| 2007 |
Rab3A deletion reduces vesicle docking (26% reduction) and quantal release (27% reduction in quantal content, 28% reduction in mini frequency) at the mouse diaphragm neuromuscular junction; Ca2+ sensitivity (not cooperativity) of release is affected. |
rab3A-null mice, electron microscopy, focal electrophysiological recordings, Ca2+ concentration-response |
Neuroscience |
High |
17640821
|
| 2008 |
FLJ13130 (TBC domain protein) is a novel Rab3A-GAP: its expression promotes GTPase activity of Rab3A in vitro and reduces GTP-Rab3A levels in living cells; a catalytically inactive R134K mutant is ineffective; FLJ13130 also acts on Rab22A, Rab27A, and Rab35 but not Rab2A or Rab6A. |
Cell-based screen for Rab3A exclusion from dense-core vesicles, in vitro GTPase activity assay, catalytic mutant control |
Genes to cells |
High |
19077034
|
| 2009 |
APP anterograde transport vesicles contain kinesin-1C, Rab3A, and a specific subset of presynaptic proteins; assembly of kinesin-1C and APP in this vesicle requires Rab3A GTPase activity, as shown by immunoisolation and time-lapse analysis. |
Time-lapse microscopy, immunoisolation of transport vesicles, GTPase-deficient Rab3A mutant analysis |
The Journal of neuroscience |
High |
19923287
|
| 2009 |
Epac activates Rab3A (promotes GDP→GTP exchange) in human sperm downstream of cAMP/Epac/Rap1/PLC signaling during acrosomal exocytosis; recombinant Epac does not directly exchange GDP from Rab3A in vitro, indicating an indirect GEF activation pathway. |
GTP/GDP loading assay in sperm, recombinant Epac in vitro exchange assay, pharmacological inhibitors |
The Journal of biological chemistry |
High |
19546222
|
| 2009 |
SNAP-29 interacts with Rab3A in a GTP-dependent manner (yeast two-hybrid and coimmunoprecipitation); coexpression of SNAP-29 and Rab3A redistributes cytoplasmic SNAP-29 and enhances surface-directed trafficking of myelin proteolipid protein, placing Rab3A upstream of SNAP-29-mediated membrane fusion. |
Yeast two-hybrid, co-immunoprecipitation, HEK293 trafficking assay |
Journal of neuroscience research |
Medium |
19170188
|
| 2010 |
Mass spectrometry and quantitative immunoblotting identify Rab3A (along with Rab3b, Rab3c, Rab27b) as exocytotic Rab machinery on synaptic vesicles; Rab3A readily dissociates from SVs during Ca2+-triggered exocytosis and is susceptible to GDI-mediated membrane extraction, whereas Rab27b persists on vesicle membranes after stimulation. |
High-resolution mass spectrometry, iTRAQ chemical labeling, quantitative immunoblotting, fluorescence microscopy, stimulation and GDI extraction assay |
The Journal of neuroscience |
High |
20926670
|
| 2011 |
Myo5a (myosin-Va) tail directly interacts with GTP-bound Rab3A on synaptic vesicles: the interaction requires GTP (not GDP or nucleotide-free Rab3A), is demonstrated by sedimentation velocity analytical ultracentrifugation, GST pulldown from synaptosomes, and in vitro motility assays requiring Rab GTPase activity. |
Analytical ultracentrifugation (sedimentation velocity), GST pulldown from synaptosomes, in vitro motility assay in squid axoplasm |
The Journal of biological chemistry |
High |
21349835
|
| 2011 |
Rab3A cycle (via RIM interaction) is coupled with Munc13-1 activation for vesicle priming; Munc18-1 promotes Rab3A dissociation from vesicles and acts downstream of the Munc13-1/RIM/Rab3A complex to enable vesicle priming and fusion. |
Rab3A overexpression/knockdown, Munc13-1/Munc18-1 co-expression, secretion assays in neuroendocrine cells |
Traffic |
Medium |
21689256
|
| 2012 |
RIM, Munc13, and Rab3A are all present in human sperm acrosomal region and participate in a pre-fusion docking step during acrosomal exocytosis; sequestering RIM or Rab3A (by antibody or recombinant protein) impairs docking of the acrosomal membrane to the plasma membrane. |
Immunostaining, functional inhibition with antibodies/recombinant proteins, transmission electron microscopy of docking |
Experimental cell research |
Medium |
22248876
|
| 2012 |
Rab3A delivers synaptic vesicles to Ca2+-dependent release sites at ribbon synapses in photoreceptors; GTPase-deficient Rab3A blocks synaptic release in an activity-dependent, frequency-dependent manner by competing with vesicles for resupply to release sites; ribbon binding and dissociation are governed by the GTP hydrolysis cycle. |
Fluorescent Rab3A delivery via patch pipette, GTPase-deficient mutant expression, paired pre- and postsynaptic recordings |
The Journal of neuroscience |
High |
22593061
|
| 2013 |
α-Synuclein interacts with membrane-associated GTP-bound Rab3A but not cytosolic GDP-Rab3A; GTPase-deficient Rab3A mutant, dominant-negative GDI (unable to recycle Rab3A from membranes), and Hsp90 inhibitors all increase membrane-bound α-synuclein, indicating that the GDI·Hsp90 complex controlling Rab3A recycling also regulates α-synuclein membrane association. |
Density gradient sedimentation, co-immunoprecipitation, GTPase-deficient mutant, dominant-negative GDI, Hsp90 inhibitors |
The Journal of biological chemistry |
High |
23344955
|
| 2013 |
β-Adrenergic receptor activation via cAMP/Epac increases the Rab3A–RIM1α association and redistributes synaptic vesicles closer to the presynaptic membrane to potentiate glutamate release, independently of PKA. |
Co-immunoprecipitation, synaptic vesicle redistribution by EM, glutamate release assay in cerebrocortical synaptosomes |
The Journal of biological chemistry |
Medium |
24036110
|
| 2015 |
ARF6 activation during acrosomal exocytosis increases GDP→GTP exchange on Rab3A (a prerequisite for exocytosis), acting via PLC/PIP2 signaling; ARF6 thus functions upstream of Rab3A in the acrosomal exocytosis cascade. |
GTP/GDP loading assay on Rab3A in sperm, pulldown assays, permeabilized sperm exocytosis, ARF6 inhibition |
The Journal of biological chemistry |
Medium |
25713146
|
| 2016 |
Rab3A partially localizes to peripheral lysosomes and is required for lysosome positioning and plasma membrane repair (PMR); Rab3A forms a complex with its effectors Slp4-a (synaptotagmin-like protein 4a) and non-muscle myosin heavy chain IIA (NMHC IIA) to position lysosomes at the cell periphery for exocytosis and PMR. |
siRNA screen of Rab family, Rab3A silencing, lysosome localization by imaging, PMR assay (streptolysin-O), co-immunoprecipitation identifying NMHC IIA as effector |
The Journal of cell biology |
High |
27325790
|
| 2016 |
Mutant huntingtin (mHtt) associates with Rab3A and prevents GTP-Rab3A from binding Rab3-GAP1, disrupting GTP→GDP conversion; this impairs BDNF vesicle docking on astrocyte plasma membranes; Rab3A overexpression rescues BDNF vesicle docking and secretion in HD astrocytes. |
Co-immunoprecipitation of mHtt and Rab3A, BDNF vesicle docking assay, Rab3A overexpression rescue in HD knock-in astrocytes |
The Journal of neuroscience |
High |
27559163
|
| 2018 |
O-GlcNAcylation of Rab3A attenuates its GTP-binding activity and suppresses its effects on mitochondrial oxidative phosphorylation and hepatocellular carcinoma cell metastasis; O-GlcNAcylation and Rab3A have opposing functional effects on these processes. |
O-GlcNAc modification identification, GTP-binding assay, in vitro and in vivo metastasis assays, mitochondrial OXPHOS measurement |
Cell death & disease |
Medium |
30237463
|
| 2021 |
Rab11 regulates Ca2+-induced lysosome exocytosis via a cascade involving Rab3A: Rab11-positive vesicles transiently interact with peripheral lysosomes; Rab11 binds GRAB (Rab3A GEF) and Rab3A, suggesting a Rab11→GRAB→Rab3A signaling cascade for lysosome exocytosis. |
siRNA silencing of Rab11a/b, live imaging of Rab11–lysosome interactions, co-immunoprecipitation of Rab11 with GRAB and Rab3A, lysosome exocytosis assay |
Journal of cell science |
Medium |
34100549
|