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Vesicle-associated membrane protein 3

Vesicle-Associated Membrane Protein 3, VAMP3
Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. This gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Because of its high homology to other known VAMPs, its broad tissue distribution, and its subcellular localization, the protein encoded by this gene was shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: VAMP2, SNAP-23, VAMP8, v-SNARE, VAMP7
Papers using Vesicle-Associated Membrane Protein 3 antibodies
Subcompartments of the macrophage recycling endosome direct the differential secretion of IL-6 and TNFα
Stow Jennifer L. et al., In The Journal of Cell Biology, 2003
... BD Biosciences), monoclonal antibody to TfnR (Zymed Laboratories and Invitrogen), and a polyclonal rabbit antibody to VAMP3 (Abcam).
Identification and localization of two brefeldin A-inhibited guanine nucleotide-exchange proteins for ADP-ribosylation factors in a macromolecular complex
Ma Dzwokai et al., In The Journal of Cell Biology, 1999
... of Leeds, Leeds, England, UK; Abcam), CIMPR (BioLegend), Lamp1 (Developmental Studies Hybridoma Bank), EEA1 (Sigma-Aldrich), VAMP3 (Synaptic Systems GmbH), and syntaxin 10 ...
Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells.
Bassham Diane, In PLoS ONE, 1993
... Polyclonal αVAMP3 antibody was from Synaptic Systems, Germany ...
Papers on Vesicle-Associated Membrane Protein 3
Expression and cellular function of vSNARE proteins in brain astrocytes.
Li et al., Paris, France. In Neuroscience, 27 Nov 2015
Astrocytic vesicles expressing VAMP2 and VAMP3 vesicular SNARE (vSNARE) proteins have been suggested to be a key feature of the tripartite synapse and mediate gliotransmitter release through Ca(2+)-regulated exocytosis.
Migration Speed of Cajal-Retzius Cells Modulated by Vesicular Trafficking Controls the Size of Higher-Order Cortical Areas.
Pierani et al., Paris, France. In Curr Biol, 05 Nov 2015
CR migration speed is cell autonomously modulated by vesicle-associated membrane protein 3 (VAMP3), a classically non-neuronal mediator of endosomal recycling.
Effects of simulated microgravity on the expression of presynaptic proteins distorting the GABA/glutamate equilibrium - a proteomics approach.
Deng et al., Beijing, China. In Proteomics, 11 Oct 2015
Microgravity induces difficulty in the formation of the SNARE complex due to the down-regulation of vesicle-associated membrane protein 3 (VAMP3) and syntaxin-1A.
Toll-like receptor 9 trafficking and signaling for type I interferons requires PIKfyve activity.
Iwasaki et al., New Haven, United States. In Int Immunol, Sep 2015
Signaling from these TLRs bifurcate at the level of distinct endosomal compartments, namely VAMP3(+) and LAMP(+) endosomes, to mediate the induction of cytokine and type I interferon (IFN) genes, respectively.
Shiga toxin stimulates clathrin-independent endocytosis of the VAMP2, VAMP3 and VAMP8 SNARE proteins.
Johannes et al., Paris, France. In J Cell Sci, Sep 2015
The SNARE proteins VAMP2, VAMP3 and VAMP8 are internalized in a clathrin-dependent manner.
The small GTPase Rab8 interacts with VAMP-3 to regulate the delivery of recycling T-cell receptors to the immune synapse.
Baldari et al., Siena, Italy. In J Cell Sci, Aug 2015
This could be accounted for by the inability of the vesicular (v)-SNARE VAMP-3 to cluster at the immune synapse in the absence of functional Rab8, which is responsible for its recruitment.
Astrocyte VAMP3 vesicles undergo Ca2+ -independent cycling and modulate glutamate transporter trafficking.
Ropert et al., Paris, France. In J Physiol, Aug 2015
ABSTRACT: Previous studies suggest that small synaptic-like vesicles in astrocytes carry vesicle-associated vSNARE proteins, VAMP3 (cellubrevin) and VAMP2 (synaptobrevin 2), both contributing to the Ca(2+) -regulated exocytosis of gliotransmitters, thereby modulating brain information processing.
Characterization of VAMP isoforms in 3T3-L1 adipocytes: implications for GLUT4 trafficking.
Gould et al., Glasgow, United Kingdom. In Mol Biol Cell, Mar 2015
The t-SNARE complex consists of Syntaxin4 and SNAP23, and whereas many studies identify VAMP2 as the v-SNARE, others suggest that either VAMP3 or VAMP8 may also fulfil this role.
Differential Effects of Munc18s on Multiple Degranulation-Relevant Trans-SNARE Complexes.
Kumar et al., Hattiesburg, United States. In Plos One, Dec 2014
We report the identification of at least six distinct trans-SNARE complexes under enhanced tethering conditions: i) VAMP2/syntaxin3/SNAP-23, ii) VAMP2/syntaxin4/SNAP-23, iii) VAMP3/syntaxin3/SNAP-23, iv) VAMP3/syntaxin4/SNAP-23, v) VAMP8/syntaxin3/SNAP-23, and vi) VAMP8/syntaxin4/SNAP-23.
Regulated delivery of molecular cargo to invasive tumour-derived microvesicles.
D'Souza-Schorey et al., United States. In Nat Commun, Dec 2014
Here we demonstrate that in amoeboid-like invasive tumour cell lines, the v-SNARE, VAMP3, regulates delivery of microvesicle cargo such as the membrane-type 1 matrix metalloprotease (MT1-MMP) to shedding microvesicles.
TLR signals induce phagosomal MHC-I delivery from the endosomal recycling compartment to allow cross-presentation.
Blander et al., New York City, United States. In Cell, Aug 2014
Instead, MHC-I are recruited from an endosomal recycling compartment (ERC), which is marked by Rab11a, VAMP3/cellubrevin, and VAMP8/endobrevin and holds large reserves of MHC-I.
Diverse autophagosome membrane sources coalesce in recycling endosomes.
Rubinsztein et al., Cambridge, United Kingdom. In Cell, 2013
mATG9- and ATG16L1-containing vesicles traffic to recycling endosomes, where VAMP3-dependent heterotypic fusions occur.
The molecular basis for the endocytosis of small R-SNAREs by the clathrin adaptor CALM.
Owen et al., Cambridge, United Kingdom. In Cell, 2011
Here, we show that the R-SNAREs VAMP8, VAMP3, and VAMP2, which cycle between the plasma membrane and endosomes, bind directly to the ubiquitously expressed, PtdIns4,5P(2)-binding, endocytic clathrin adaptor CALM/PICALM.
VAMP3 regulates podosome organisation in macrophages and together with Stx4/SNAP23 mediates adhesion, cell spreading and persistent migration.
Murray et al., Sydney, Australia. In Exp Cell Res, 2011
This important SNARE complex facilitates macrophage adhesion, spreading, and persistent macrophage migration on fibronectin through the delivery of VAMP3-positive membrane with its cargo to expand the plasma membrane.
VAMP3 is associated with endothelial weibel-palade bodies and participates in their Ca(2+)-dependent exocytosis.
Gerke et al., Münster, Germany. In Biochim Biophys Acta, 2011
Endothelial cells specifically select VAMP 3 over VAMP8 to cooperate with syntaxin 4 and SNAP23 in the Ca(2+)-triggered fusion of Weibel-Palade bodies with the plasma membrane.
Transport of the major myelin proteolipid protein is directed by VAMP3 and VAMP7.
Krämer-Albers et al., Mainz, Germany. In J Neurosci, 2011
VAMP3 mediates fusion of recycling endosome-derived vesicles with the oligodendroglial plasma membrane in the course of the secretory pathway
TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways.
Colombo et al., San Martín, Argentina. In Biochim Biophys Acta, 2009
TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways.
VAMP3, syntaxin-13 and SNAP23 are involved in secretion of matrix metalloproteinases, degradation of the extracellular matrix and cell invasion.
Coppolino et al., Guelph, Canada. In J Cell Sci, 2009
the importance of VAMP3 in the trafficking of matrix metalloproteinases during degradation of extracellular matrix substrates and subsequent cellular invasion
A role for the phagosome in cytokine secretion.
Stow et al., Brisbane, Australia. In Science, 2006
Tumor necrosis factor alpha (TNFalpha) is trafficked from the Golgi to the recycling endosome (RE), where vesicle-associated membrane protein 3 mediates its delivery to the cell surface at the site of phagocytic cup formation.
Role of SNARE's in the GLUT4 translocation response to insulin in adipose cells and muscle.
Cushman et al., Bethesda, United States. In J Basic Clin Physiol Pharmacol, 1997
VAMP2 and VAMP3/cellubrevin (v-SNARE's) have been shown to interact with the t-SNARE's syntaxin 4 and SNAP-23.
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