Vesicle-associated membrane protein-2 (synaptobrevin-2) forms a complex with synaptophysin [PDF]
Biochemical Journal, 1995 Vesicle-associated membrane protein (VAMP) (or synaptobrevin), a type II membrane protein of small synaptic vesicles, is essential for neuroexocytosis because its proteolysis by tetanus and botulinum neurotoxins types B, D, F and G blocks neurotransmitter release.
P, Washbourne, G, Schiavo, C, Montecucco
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Sept8 controls the binding of vesicle‐associated membrane protein 2 to synaptophysin [PDF]
Journal of Neurochemistry, 2009 AbstractSeptins, a conserved family of GTP/GDP‐binding proteins, are present in organisms as diverse as yeast and mammals. We analyzed the distribution of five septins, Sept6, Sept7, Sept8, Sept9 and Sept11, in various rat tissues by western blot analyses and found all septins to be expressed in brain.
Hidenori, Ito +10 more
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Characterization of an alternatively spliced isoform of rat vesicle associated membrane protein‐2 (VAMP‐2) [PDF]
FEBS Letters, 1999 VAMPs are esicle ssociated embrane roteins that are essential for secretion. A spliced isoform of rat VAMP‐2, called VAMP‐2B, is characterized in this study. The VAMP‐2B transcript is the result of alternative RNA splicing in which an intron is retained.
Mandic, Robert, Lowe, Anson W.
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Synaptotagmin 4 and 5 additively contribute to Arabidopsis immunity to Pseudomonas syringae DC3000
Plant Signaling & Behavior, 2022 Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) are essential for vesicle trafficking in plants. Vesicle-associated membrane protein 721 and 722 (VAMP721/722) are secretory vesicle-localized R-SNAREs, which are involved in
Soohong Kim +3 more
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The function of VAMP2 in mediating membrane fusion: An overview
Frontiers in Molecular Neuroscience, 2022 Vesicle-associated membrane protein 2 (VAMP2, also known as synaptobrevin-2), encoded by VAMP2 in humans, is a key component of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex.
Chong Yan +4 more
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Two Rab proteins, vesicle-associated membrane protein 2 (VAMP-2) and secretory carrier membrane proteins (SCAMPs), are present on immunoisolated parietal cell tubulovesicles [PDF]
Biochemical Journal, 1997 The tubulovesicles of gastric parietal cells sequester H+/K+-ATPase molecules within resting parietal cells. Stimulation of parietal cell secretion elicits delivery of intracellular H+/K+-ATPase to the apically oriented secretory canaliculus. Previous investigations have suggested that this process requires the regulated fusion of intracellular ...
B C, Calhoun, J R, Goldenring
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Identification of Myelin Basic Protein Proximity Interactome Using TurboID Labeling Proteomics
Cells, 2023 Myelin basic protein (MBP) is one of the key structural elements of the myelin sheath and has autoantigenic properties in multiple sclerosis (MS).
Evgeniya V. Smirnova +6 more
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Complexin 2 Modulates Vesicle-associated Membrane Protein (VAMP) 2-regulated Zymogen Granule Exocytosis in Pancreatic Acini [PDF]
Journal of Biological Chemistry, 2010 Complexins are soluble proteins that regulate the activity of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes necessary for vesicle fusion. Neuronal specific complexin 1 has inhibitory and stimulatory effects on exocytosis by clamping trans-SNARE complexes in a prefusion state and promoting conformational changes
Michelle A, Falkowski +2 more
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Different regions of synaptic vesicle membrane regulate VAMP2 conformation for the SNARE assembly
Nature Communications, 2020 Vesicle associated membrane protein 2 (VAMP2) contains a conserved SNARE motif that interacts with syntaxin-1 and SNAP25 for SNARE complex assembly. Here authors use in-cell NMR spectroscopy to describe the dynamic membrane association of VAMP2 SNARE ...
Chuchu Wang +15 more
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Vesicle-associated Membrane Protein-2 (VAMP2) Mediates cAMP-stimulated Renin Release in Mouse Juxtaglomerular Cells [PDF]
Journal of Biological Chemistry, 2011 Renin is essential for blood pressure control. Renin is stored in granules in juxtaglomerular (JG) cells, located in the pole of the renal afferent arterioles. The second messenger cAMP stimulates renin release. However, it is unclear whether fusion and exocytosis of renin-containing granules is involved.
Mendez, Mariela +4 more
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