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Vesicle-associated membrane protein 1

Synaptobrevin, VAMP-1, synaptobrevin I, synaptobrevin 1
plays a role in protein transport to the plasma membrane [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: SNAP-25, VAMP2, CAN, Synaptophysin, ACID
Papers using Synaptobrevin antibodies
Class II Phosphoinositide 3-Kinase Regulates Exocytosis of Insulin Granules in Pancreatic β Cells*
Maffucci Tania et al., In The Journal of Biological Chemistry, 2007
... The anti-VAMP1/2/3 used in confocal microscopy analysis was from Santa Cruz Biotechnology (Santa Cruz, CA) ...
A homeodomain protein code specifies progenitor cell identity and neuronal fate in the ventral neural tube
Laufer Ed et al., In Neural Development, 1999
... Rabbit anti-synaptophysin 1:500 (Zymed); goat anti-vesicular acetylcholine transporter (VAChT) (Zymed) 1:1,000; mouse anti-VAMP2/synaptobrevin 1:1,000 (Synaptic Systems) [ ...
Mapping of R-SNARE function at distinct intracellular GLUT4 trafficking steps in adipocytes
Pessin Jeffrey E. et al., In The Journal of Cell Biology, 1998
... VAMP1, 3, 4, and 7 polyclonal antibodies were purchased from Novus Biologicals.
Papers on Synaptobrevin
Phosphatidylserine-Dependent Catalysis of Stalk and Pore Formation by Synaptobrevin JMR-TMD Peptide.
Lentz et al., Chapel Hill, United States. In Biophys J, Dec 2015
Here, we performed experiments with highly curved vesicles brought into contact using low concentrations of polyethylene glycol (PEG) to investigate the influence of the synaptobrevin (SB) TMD with an attached JMR (SB-JMR-TMD) on the rates of stalk and pore formation during vesicle fusion.
Vesicular Synaptobrevin/VAMP2 Levels Guarded by AP180 Control Efficient Neurotransmission.
Maritzen et al., Berlin, Germany. In Neuron, Nov 2015
Neurotransmission depends on synaptic vesicle (SV) exocytosis driven by soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex formation of vesicular synaptobrevin/VAMP2 (Syb2).
Ubiquitin-Synaptobrevin Fusion Protein Causes Degeneration of Presynaptic Motor Terminals in Mice.
Lin et al., Dallas, United States. In J Neurosci, Sep 2015
We engineered transgenic mice expressing a fusion protein, consisting of the following: (1) Ub(G76V), GFP, and a synaptic vesicle protein synaptobrevin-2 (Ub(G76V)-GFP-Syb2); (2) GFP-Syb2; or (3) Ub(G76V)-GFP-Syntaxin1, all under the control of a neuron-specific Thy-1 promoter.
Synaptobrevin Transmembrane Domain Dimerization Studied by Multiscale Molecular Dynamics Simulations.
Böckmann et al., Erlangen, Germany. In Biophys J, Sep 2015
Synaptic vesicle fusion requires assembly of the SNARE complex composed of SNAP-25, syntaxin-1, and synaptobrevin-2 (sybII) proteins.
Synaptobrevin transmembrane domain influences exocytosis by perturbing vesicle membrane curvature.
Jackson et al., Madison, United States. In Biophys J, Aug 2015
In this study, we explored the possibility of manipulating C0 by mutating the transmembrane domain (TMD) of the vesicle membrane protein synaptobrevin 2 (syb2).
Activity of botulinum neurotoxin type D (strain 1873) in human neurons.
Johnson et al., Madison, United States. In Toxicon, Jul 2015
In vitro data indicate that BoNT/D does not cleave human VAMP1 efficiently, and differential expression of the VAMP 1 and 2 isoforms may be responsible for the above observations.
Genetically-controlled Vesicle-Associated Membrane Protein 1 expression may contribute to Alzheimer's pathophysiology and susceptibility.
Belbin et al., Jacksonville, United States. In Mol Neurodegener, 2014
RESULTS: Here we report 5 polymorphisms in Vesicle-Associated Membrane Protein 1 (VAMP1), a gene encoding a member of the SNARE complex, associated with bidirectionally altered cerebellar VAMP1 transcript levels (all p<0.05).
Postsynaptic VAMP/Synaptobrevin Facilitates Differential Vesicle Trafficking of GluA1 and GluA2 AMPA Receptor Subunits.
Davanger et al., Oslo, Norway. In Plos One, 2014
We demonstrate that they harbor vesicle-associated membrane protein 2 (VAMP2/synaptobrevin-2) and glutamate receptor subunit 1 (GluA1).
The Synaptic Vesicle Release Machinery.
Xu et al., Dallas, United States. In Annu Rev Biophys, 2014
The SNAREs Syntaxin-1, Synaptobrevin, and SNAP-25 play a central role in membrane fusion, forming SNARE complexes that bridge the vesicle and plasma membranes and that are disassembled by NSF-SNAPs.
Architecture of the Synaptophysin/Synaptobrevin Complex: Structural Evidence for an Entropic Clustering Function at the Synapse.
Stowell et al., Boulder, United States. In Sci Rep, 2014
We have purified the mammalian synaptophysin/synaptobrevin (SYP/VAMP2) complex to homogeneity in the presence of cholesterol and determined the 3D EM structure by single particle reconstruction.
The Sybtraps: control of synaptobrevin traffic by synaptophysin, α-synuclein and AP-180.
Cousin et al., Edinburgh, United Kingdom. In Traffic, 2014
Synaptobrevin II (sybII) is a key fusogenic molecule on synaptic vesicles (SVs) therefore the active maintenance of both its conformation and location in sufficient numbers on this organelle is critical in both mediating and sustaining neurotransmitter release.
Structural and functional analysis of tomosyn identifies domains important in exocytotic regulation.
Stuenkel et al., Ann Arbor, United States. In J Biol Chem, 2011
multiple domains outside the R-SNARE of tomosyn are critical to the efficacy of inhibition by tomosyn on exocytotic secretion
VAMP-1, VAMP-2, and syntaxin-4 regulate ANP release from cardiac myocytes.
Lowenstein et al., Baltimore, United States. In J Mol Cell Cardiol, 2010
Syntaxin-4 and VAMP-1 and VAMP-2 regulate cardiac myocyte exocytosis of ANP.
A coiled coil trigger site is essential for rapid binding of synaptobrevin to the SNARE acceptor complex.
Fasshauer et al., Göttingen, Germany. In J Biol Chem, 2010
the trigger site in synaptobrevin is crucial for productive SNARE zippering
Effect of monolayer lipid charges on the structure and orientation of protein VAMP1 at the air-water interface.
Oda et al., Pessac, France. In Biochim Biophys Acta, 2010
Data report the structure and the assembling behavior of VAMP1 incorporated in a lipid monolayer at an air-water interface which mimics the membrane environment, and show that the structure of VAMP1 is clearly controlled by protein-lipid interactions.
Identification of a novel Vamp1 splice variant in the cochlear nucleus.
Popper et al., Milwaukee, United States. In Hear Res, 2008
Several species of Vamp1 were amplified from a brain cDNA library including a full length clone of Vamp1as and a novel splice variant we termed Vamp1nv that was expressed in each of the cochlear nucleus subdivisions.
Altered complexin expression in psychiatric and neurological disorders: cause or consequence?
Brose, Göttingen, Germany. In Mol Cells, 2008
They operate by binding to trimeric SNARE complexes consisting of the vesicle protein Synaptobrevin and the plasma membrane proteins Syntaxin and SNAP-25, which are key executors of membrane fusion reactions.
Synaptobrevin is essential for fast synaptic-vesicle endocytosis.
Kavalali et al., United States. In Nat Cell Biol, 2004
Synaptobrevin-2 (VAMP-2), the major SNARE protein of synaptic vesicles, is required for fast calcium-triggered synaptic-vesicle exocytosis.
Roles of SNARE proteins and synaptotagmin I in synaptic transmission: studies at the Drosophila neuromuscular synapse.
Kidokoro, Maebashi, Japan. In Neurosignals, 2003
The roles of SNARE proteins, i.e. neuronal Synaptobrevin (n-Syb), SNAP-25 and Syntaxin 1A (Syx 1A), and Synaptotagmin I (Syt I) in synaptic transmission have been studied in situ using mutant embryos or larvae that lack these molecules or have alterations in them.
Ypt1p implicated in v-SNARE activation.
Ferro-Novick et al., New Haven, United States. In Nature, 1995
Synaptobrevin-like membrane proteins that reside on transport vesicles, called the vesicle SNARE (v-SNARE), play a key role in ensuring that a vesicle targets and fuses with its correct acceptor compartment.
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