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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
Association between DNA methylation and multidrug resistance in human glioma SHG‑44 cells.
Wang et al., Chongqing, China. In Mol Med Report, 31 Jan 2015
Genes including SNAP47, VAMP4 and VAMP3 may serve as the downstream effectors of Pgp, COX‑2 or PKCα; however, further experiments are required to verify these observations.
Genetic Evidence for PLASMINOGEN as a Shared Genetic Risk Factor of Coronary Artery Disease and Periodontitis.
Schreiber et al., Kiel, Germany. In Circ Cardiovasc Genet, 02 Jan 2015
BACKGROUND: -Genetic studies demonstrated the presence of risk alleles in the genes ANRIL and CAMTA1/VAMP3 that are shared between coronary artery disease (CAD) and periodontitis.
Human herpesvirus 6 gM/gN complex interacts with v-SNARE in infected cells.
Mori et al., Kōbe, Japan. In J Gen Virol, 31 Dec 2014
Liquid chromatography-MS/MS analysis showed that the HHV-6 gM/gN complex interacts with the v-SNARE protein, vesicle-associated membrane protein 3 (VAMP3).
Proteomic analysis of gliosomes from mouse brain: identification and investigation of glial membrane proteins.
Verheijen et al., In J Proteome Res, 13 Nov 2014
Interestingly, gliosome preparations were found to be enriched for different classes of known astrocyte proteins, such as VAMP3 (involved in astrocyte exocytosis), Ezrin (perisynaptic astrocyte cytoskeletal protein), and Basigin (astrocyte membrane glycoprotein), as well as for G-protein mediated signaling proteins.
Endosomal sorting of VAMP3 is regulated by PI4K2A.
Balla et al., Toronto, Canada. In J Cell Sci, Oct 2014
In this study, we identified phosphatidylinositol 4-kinase IIα (PI4K2A) as a binding partner of vesicle-associated membrane protein 3 (VAMP3), a small R-SNARE involved in recycling and retrograde transport, and found that the two proteins co-reside on tubulo-vesicular endosomes.
Role of VAMP3 and VAMP7 in the commitment of Yersinia pseudotuberculosis to LC3-associated pathways involving single- or double-membrane vacuoles.
Lafont et al., Lille, France. In Autophagy, Sep 2014
Second, in these cells, we unexpectedly found that VAMP3 localizes preferentially to Yersinia-containing vacuoles (YCVs) with single membranes using correlative light-electron microscopy.
Vesicle-associated membrane protein 2 (VAMP2) but Not VAMP3 mediates cAMP-stimulated trafficking of the renal Na+-K+-2Cl- co-transporter NKCC2 in thick ascending limbs.
Ortiz et al., Detroit, United States. In J Biol Chem, Sep 2014
In vivo silencing of VAMP2 but not VAMP3 in TALs blunted cAMP-stimulated steady-state surface NKCC2 expression and completely blocked cAMP-stimulated NKCC2 exocytic delivery.
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.
Differential regulation of the serotonin transporter by vesicle-associated membrane protein 2 in cells of neuronal versus non-neuronal origin.
Wiborg et al., Århus, Denmark. In Plos One, Dec 2013
The related isoforms VAMP1 and VAMP3 also physically interact with SERT.
Characterization of novel markers of senescence and their prognostic potential in cancer.
Macip et al., Leicester, United Kingdom. In Cell Death Dis, Dec 2013
We identified 107 proteins that could be potential markers of senescence and validated 10 of them (DEP1, NTAL, EBP50, STX4, VAMP3, ARMX3, B2MG, LANCL1, VPS26A and PLD3).
PICALM modulates autophagy activity and tau accumulation.
Rubinsztein et al., Cambridge, United Kingdom. In Nat Commun, Dec 2013
CALM influences autophagy by regulating the endocytosis of SNAREs, such as VAMP2, VAMP3 and VAMP8, which have diverse effects on different stages of the autophagy pathway, from autophagosome formation to autophagosome degradation.
Diverse autophagosome membrane sources coalesce in recycling endosomes.
Rubinsztein et al., Cambridge, United Kingdom. In Cell, Oct 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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