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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)
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Papers using
Vesicle-Associated Membrane Protein 3
antibodies
Subcompartments of the macrophage recycling endosome direct the differential secretion of IL-6 and TNFα
Supplier
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
Supplier
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.
Supplier
In PLoS ONE, 1993
... Polyclonal αVAMP3 antibody was from Synaptic Systems, Germany ...
Papers on
Vesicle-Associated Membrane Protein 3
Crohn's disease loci are common targets of protozoa-driven selection.
New
Italy. In Mol Biol Evol, 31 May 2013
Pathway analysis indicated that ARHGEF2 and NSF participate in a molecular network, which also contains VAMP3 (previously associated to CD) and is centered around miR-31 (known to be disregulated in CD).
Sutherlandia frutescens prevents changes in diabetes-related gene expression in a fructose-induced insulin resistant cell model.
New
Port Elizabeth, South Africa. In J Ethnopharmacol, Apr 2013
The gene VAMP3, which plays a role in vesicle transport, was down-regulated by insulin resistance, and up-regulated by Sutherlandia frutescens.
Goliath family E3 ligases regulate the recycling endosome pathway via VAMP3 ubiquitylation.
New
Umeå, Sweden. In Embo J, Mar 2013
We show that the soluble N-ethylmaleimide-sensitive fusion attachment protein receptor (SNARE) protein VAMP3 is a target of these ubiquitin ligases, and that recycling endosome trafficking is abrogated in response to their activity.
Overexpression of vesicle-associated membrane protein (VAMP) 3, but not VAMP2, protects glucose transporter (GLUT) 4 protein translocation in an in vitro model of cardiac insulin resistance.
New
Maastricht, Netherlands. In J Biol Chem, Nov 2012
Here, we investigated whether overexpression of VAMP2 and/or VAMP3 could protect insulin-stimulated GLUT4 translocation under conditions of insulin resistance.
Silencing of VAMP3 expression does not affect Brucella melitensis infection in mouse macrophages.
New
Mexico City, Mexico. In Virulence, Sep 2012
Vesicle-associated membrane protein 3 (VAMP3) is a v-SNARE protein that promotes the exocytosis of the proinflammatory cytokine TNF at the phagocytic cup when docking to its cognate t-SNARE proteins syntaxin-4 and SNAP-23 at the plasma membrane.
Regulation of integrin endocytic recycling and chemotactic cell migration by syntaxin 6 and VAMP3 interaction.
New
Louisville, United States. In J Cell Sci, Sep 2012
In STX6-depleted cells, α3β1 integrin is accumulated in recycling endosomes that contain the v-SNARE VAMP3.
Granule exocytosis is required for platelet spreading: differential sorting of α-granules expressing VAMP-7.
New
Boston, United States. In Blood, Aug 2012
Immunofluorescence microscopy demonstrated that granules expressing VAMP-3 and VAMP-8 localized to the central granulomere of spread platelets along with the granule cargos von Willebrand factor and serotonin.
SNARE proteins are not excessive for the formation of post-Golgi SNARE complexes in HeLa cells.
New
Tōbetsu, Japan. In Mol Cell Biochem, Jul 2012
To evaluate the role of SNARE proteins in the constitutive exocytosis, we knocked down syntaxin 3, 4, 5, 6, 7, and VAMP3, 5, 7, 8 with their siRNAs, and determined the cell-to-medium ratio of CLuc, a secreted luciferase of Cypridina noctiluca.
Genome-wide association study of periodontal pathogen colonization.
New
Chapel Hill, United States. In J Dent Res, Jul 2012
However, 13 loci, including KCNK1, FBXO38, UHRF2, IL33, RUNX2, TRPS1, CAMTA1, and VAMP3, provided suggestive evidence (p < 5 × 10(-6)) of association.
Anoctamin 1 (Tmem16A) Ca2+-activated chloride channel stoichiometrically interacts with an ezrin-radixin-moesin network.
New
San Luis Potosí, Mexico. In Proc Natl Acad Sci U S A, Jul 2012
Another network associated with Ano1 includes the SNARE and SM proteins VAMP3, syntaxins 2 and -4, and syntaxin-binding proteins munc18b and munc18c, which are integral to translocation of vesicles to the plasma membrane.
Specificity of botulinum protease for human VAMP family proteins.
New
Ōsaka, Japan. In Microbiol Immunol, Apr 2012
Kinetic analysis revealed that all LC have higher affinity and catalytic activity for the non-neuronal SNARE isoform VAMP3 than for the neuronal VAMP1 and 2 isoforms.
VAMP8 is a vesicle SNARE that regulates mucin secretion in airway goblet cells.
New
Chapel Hill, United States. In J Physiol, Mar 2012
Unlike VAMP8 silencing, knockdown of VAMP2 or VAMP3 did not affect mucin secretion.
The molecular basis for the endocytosis of small R-SNAREs by the clathrin adaptor CALM.
Impact
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
Impact
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.
Review
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.
