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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
Supplier
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
Supplier
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.
Supplier
Bassham Diane, In PLoS ONE, 1993
... Polyclonal αVAMP3 antibody was from Synaptic Systems, Germany ...
Papers on Vesicle-Associated Membrane Protein 3
Vesicular transport system in myotubes: ultrastructural study and signposting with vesicle-associated membrane proteins.
New
Yorifuji et al., Maebashi, Japan. In Histochem Cell Biol, Apr 2014
Vesicles with VAMP2, VAMP3, or VAMP5 were found near the ends of the myotubes.
Cytomegalovirus miRNAs target secretory pathway genes to facilitate formation of the virion assembly compartment and reduce cytokine secretion.
New
Nelson et al., Beaverton, United States. In Cell Host Microbe, Apr 2014
We find that HCMV miRs UL112-1, US5-1, and US5-2 target multiple components of the host secretory pathway, including VAMP3, RAB5C, RAB11A, SNAP23, and CDC42.
SNAP-23 and VAMP-3 contribute to the release of IL-6 and TNFα from a human synovial sarcoma cell line.
New
Wang et al., Dublin, Ireland. In Febs J, Feb 2014
Here, the complement of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) in human synovial sarcoma cells (SW982) was examined with respect to the secretion of interleukin-6 (IL-6) and tumour necrosis factor α (TNFα), before and after knockdown of a synaptosome-associated protein of molecular mass 23 kDa (SNAP-23) or the vesicle-associated membrane protein 3 (VAMP-3).
ATG16L1 meets ATG9 in recycling endosomes: additional roles for the plasma membrane and endocytosis in autophagosome biogenesis.
New
Rubinsztein et al., Cambridge, United Kingdom. In Autophagy, Jan 2014
The R-SNARE VAMP3 mediates the coalescence of the 2 different pools of vesicles (containing ATG16L1 or ATG9) in recycling endosomes.
The large non-coding RNA ANRIL, which is associated with atherosclerosis, periodontitis and several forms of cancer, regulates ADIPOR1, VAMP3 and C11ORF10.
New
Schaefer et al., Kiel, Germany. In Hum Mol Genet, Dec 2013
By genome-wide expression profiling using Affymetrix HG1.0 ST Arrays, we identified the transcription of ADIPOR1, VAMP3 and C11ORF10 to be correlated with decreased ANRIL expression in a time-dependent manner.
Diverse autophagosome membrane sources coalesce in recycling endosomes.
New
Impact
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.
GHRH receptor-targeted botulinum neurotoxin selectively inhibits pulsatile GH secretion in male rats.
New
Lightman et al., Bristol, United Kingdom. In Endocrinology, Sep 2013
Here we show this TSI activates GHRH receptors in primary cultured rat pituicytes is internalized into these cells, depletes VAMP-3, and inhibits phorbol-12-myristate-13-acetate-induced GH secretion.
Crohn's disease loci are common targets of protozoa-driven selection.
New
Sironi et al., Médéa, Algeria. In Mol Biol Evol, 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
Dealtry et al., 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
Palmer et al., 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.
Luiken et al., Maastricht, Netherlands. In J Biol Chem, 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.
Verdugo-Rodríguez et al., Mexico. In Virulence, 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.
The molecular basis for the endocytosis of small R-SNAREs by the clathrin adaptor CALM.
Impact
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
Impact
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.
Review
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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