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Vesicle-associated membrane protein 2

VAMP2, vesicle-associated membrane protein 2, synaptobrevin 2
plays a role in membrane fusion in neuronal exocytosis [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: Synaptobrevin, SNAP-25, Insulin, CAN, Synaptophysin
Papers using VAMP2 antibodies
Insulin-like growth factor-I inhibits transcriptional responses of transforming growth factor-beta by phosphatidylinositol 3-kinase/Akt-dependent suppression of the activation of Smad3 but not Smad2.
Nurminsky Dmitry I., In PLoS ONE, 2002
... dehydrogenase (Abcam, ab34436), Protein Kinase C-zeta (Cell signaling, ab51157), P-PKC-zeta (Abcam, ab76129), Syntaxin 4 (Abcam, ab57841), Vamp2 (Abcam, ab3347), Vimentin (Santacruz, sc73259, ...
Analysis of amino and carboxy terminal GLUT-4 targeting motifs in 3T3-L1 adipocytes using an endosomal ablation technique.
Calbet Jose A. L., In PLoS ONE, 1998
... Anti VAMP2 and GFP mAb was from Synaptic Systems (Göttingen, Germany) ...
Akt2 phosphorylates Synip to regulate docking and fusion of GLUT4-containing vesicles
Mori Masatomo et al., In The Journal of Cell Biology, 1997
... The VAMP2 antibody was purchased from Calbiochem, and cell culture media and reagents were purchased from Life Technologies.
Phosphorylation of Munc-18/n-Sec1/rbSec1 by protein kinase C: its implication in regulating the interaction of Munc-18/n-Sec1/rbSec1 with syntaxin
Thurmond Debbie C. et al., In Diabetes, 1995
... The rabbit Syntaxin 4, mouse clathrin, mouse anti–green fluorescent protein (GFP), and mouse VAMP2 antibodies were purchased from Chemicon (Temecula, CA), BD Biosciences (Franklin Lakes, NJ), Clontech ...
Distinction between true acrosome reaction and degenerative acrosome loss by a one-step staining method using Pisum sativum agglutinin
Hughson Fred, In PLoS Biology, 1991
... Anti-VAMP2 (mouse monoclonal, clone 69.1, purified IgG), and anti-syntaxin1A (rabbit polyclonal, whole serum) were from Synaptic Systems (Göttingen, Germany) ...
Papers on VAMP2
Comparative characterization of Botulinum Neurotoxin subtypes F1 and F7 featuring differential substrate recognition and cleavage mechanisms.
Chen et al., Shenzhen, China. In Toxicon, Jan 2016
Substrate mapping and saturation mutagenesis analysis revealed that VAMP2 (20-65) was likely a minimally effective substrate for LC/F7 (light chain of BoNT/F7), and in addition, LC/F7 recognized VAMP2 in a unique way, which differed significantly from that of LC/F1, although both of them share similar substrate binding and hydrolysis mode.
Resident CAPS on dense-core vesicles docks and primes vesicles for fusion.
Martin et al., Madison, United States. In Mol Biol Cell, Jan 2016
The knockdown of CAPS by shRNA eliminated the VAMP-2-dependent docking and evoked exocytosis of fusion-competent vesicles.
Differential role of SNAP-25 phosphorylation by protein kinases a and C in the regulation of SNARE complex formation and exocytosis in PC12 cells.
Hirata et al., Fukuoka, Japan. In Cell Signal, Jan 2016
UNASSIGNED: The final step of regulated exocytosis, membrane fusion, is mediated by formation of the SNARE complex by syntaxin, SNAP-25 (synaptosomal-associated protein of 25kDa), and VAMP (vesicle-associated membrane protein).
Ketamine Inhibits ATP-Evoked Exocytotic Release of Brain-Derived Neurotrophic Factor from Vesicles in Cultured Rat Astrocytes.
Zorec et al., Ljubljana, Slovenia. In Mol Neurobiol, Jan 2016
As revealed by double-fluorescent micrographs, BDNF-pHse localized to vesicles positive for the soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) proteins, vesicle-associated membrane protein 2 (VAMP2), VAMP3, and synaptotagmin IV.
Lipid-anchored synaptobrevin provides little or no support for exocytosis or liposome fusion.
Jackson et al., United States. In J Biol Chem, Jan 2016
To test the role of membrane attachment we generated four variants of the synaptic v-SNARE synaptobrevin-2 (syb2) anchored to the membrane by lipid instead of protein.
Expression and cellular function of vSNARE proteins in brain astrocytes.
Li et al., Paris, France. In Neuroscience, 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.
Astrocytic vesicles and gliotransmitters: Slowness of vesicular release and synaptobrevin2-laden vesicle nanoarchitecture.
Parpura et al., Ljubljana, Slovenia. In Neuroscience, Mar 2015
Up to 25 molecules of synaptobrevin 2 (Sb2), a SNARE complex protein, reside at a single astroglial vesicle; an individual neuronal, i.e. synaptic, vesicle contains ∼70 Sb2 molecules.
Anchored multiplex PCR for targeted next-generation sequencing.
Le et al., Boston, United States. In Nat Med, 2014
On the basis of our experience with performing AMP on 986 clinical FFPE samples, we show its potential as both a robust clinical assay and a powerful discovery tool, which we used to identify new therapeutically important gene fusions: ARHGEF2-NTRK1 and CHTOP-NTRK1 in glioblastoma, MSN-ROS1, TRIM4-BRAF, VAMP2-NRG1, TPM3-NTRK1 and RUFY2-RET in lung cancer, FGFR2-CREB5 in cholangiocarcinoma and PPL-NTRK1 in thyroid carcinoma.
How could SNARE proteins open a fusion pore?
Lindau et al., Göttingen, Germany. In Physiology (bethesda), 2014
The SNARE (Soluble NSF Attachment protein REceptor) complex, which in mammalian neurosecretory cells is composed of the proteins synaptobrevin 2 (also called VAMP2), syntaxin, and SNAP-25, plays a key role in vesicle fusion.
Ca²⁺-regulated secretory granule exocytosis in pancreatic and parotid acinar cells.
Groblewski et al., Madison, United States. In Cell Calcium, 2014
Studies indicate the early phase is triggered by Ca(2+) and involves the SG proteins VAMP2 (vesicle associated membrane protein2), Ca(2+)-sensing protein synatotagmin 1 (syt1) and the accessory protein complexin 2. The molecular details for regulation of VAMP8-mediated SG exocytosis and the prolonged phase of secretion are still emerging.
The complement inhibitor CD59 regulates insulin secretion by modulating exocytotic events.
Renström et al., Malmö, Sweden. In Cell Metab, 2014
CD59 interacts with the exocytotic proteins VAMP2 and Syntaxin-1.
Exocytosis and synaptic vesicle function.
Shin, Galveston, United States. In Compr Physiol, 2014
In synapses of the central nervous system, synaptobrevin 2, a major vesicular SNARE protein, forms a ternary SNARE complex with the plasma membrane SNARE proteins, syntaxin 1 and SNAP25.
SNARE proteins: one to fuse and three to keep the nascent fusion pore open.
Pincet et al., New Haven, United States. In Science, 2012
We found that although only one SNARE per nanodisc is required for maximum rates of bilayer fusion, efficient release of content on the physiologically relevant time scale of synaptic transmission apparently requires three or more SNARE complexes (SNAREpins) and the native transmembrane domain of vesicle-associated membrane protein 2 (VAMP2).
Reduction of vesicle-associated membrane protein 2 expression leads to a kindling-resistant phenotype in a murine model of epilepsy.
Slevin et al., Lexington, United States. In Neuroscience, 2012
microelectrode array measurements in specific hippocampal subregions of VAMP2(+/-) mice showed significant reductions in potassium-evoked glutamate release
Discovery of a novel enzymatic cleavage site for botulinum neurotoxin F5.
Barr et al., Atlanta, United States. In Febs Lett, 2012
BoNT/F5 cleaves substrate synaptobrevin-2 in a different location than the other BoNT/F subtypes, between (54)L and (55)E.
Regulation of glucose transporter translocation in health and diabetes.
Bogan, New Haven, United States. In Annu Rev Biochem, 2011
In unstimulated cells, GLUT4 is incorporated into specialized storage vesicles containing IRAP, LRP1, sortilin, and VAMP2, which are sequestered by TUG, Ubc9, and other proteins.
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.
SNARE-mediated rapid lysosome fusion in membrane raft clustering and dysfunction of bovine coronary arterial endothelium.
Li et al., Richmond, United States. In Am J Physiol Heart Circ Physiol, 2011
VAMP-2 is critical to lysosome fusion in membrane raft clustering, and this VAMP-2-mediated lysosome-MR signalosomes contribute to redox regulation of coronary endothelial function.
Synaptophysin is required for synaptobrevin retrieval during synaptic vesicle endocytosis.
Cousin et al., Edinburgh, United Kingdom. In J Neurosci, 2011
Synaptophysin controls synaptobrevin (sybII)traffic in nerve terminals during synaptic vesicle (SV) endocytosis, an interaction that may act as an adjustable regulator of SV retrieval efficiency.
VAMP-2, SNAP-25A/B and syntaxin-1 in glutamatergic and GABAergic synapses of the rat cerebellar cortex.
Ambrosi et al., Bari, Italy. In Bmc Neurosci, 2010
VAMP2, SNAP25b and syntaxin 1 characterize most cerebellar glutamatergic synapses and only one type of GABAergic synapse.
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