Vamp2 Antibody

1. our findings show an intimate interaction between the dynamics of the VAMP2 transmembrane domains via the central glycine and the fluidity of the lipid membrane. In turn, this interaction influences greatly the likelihood and speed of fusion pore opening and expansion. PMID: 28588281
2. The ternary complex of syntaxin1:SNAP25:Munc18-1binds synaptobrevin with fast kinetics, resulting in the rapid formation of a fully zippered SNARE complex to which Munc18-1 remains tethered by the N-terminal domain of syntaxin1. PMID: 28483813
3. Syp1 clears Syb2 from the presynaptic active zone to prevent short-term depression. PMID: 26854222
4. These effects weaken the integrity of the outer membrane layer and are attributed mainly to the highly charged linker and juxtamembrane regions of sybII PMID: 26851777
5. miR-206 regulates lung surfactant secretion by limiting the availability of VAMP-2 protein. PMID: 25481410
6. distribution of SNAP25, VAMP1 and VAMP2 in adult deep cerebellar nuclei differs significantly from that found in newborn DCN and administration of E2 in the newborn DCN affected synaptic density and also changed their distribution PMID: 24534378
7. a novel interaction between SERT and a synaptic vesicle protein PMID: 24878716
8. In vivo silencing of VAMP2 but not VAMP3 in TALs blunted cAMP-stimulated steady-state surface NKCC2 expression and completely blocked cAMP-stimulated NKCC2 exocytic delivery PMID: 25008321
9. We suggest that VAMP-2 is the v-SNARE (vesicle SNARE) involved in regulated surfactant secretion. PMID: 22571236
10. The Ca2+-dependent transition in syntaxin 1A (Syx) involves zippering between the membrane-proximal juxtamembrane regions of Syx and VAMP2. PMID: 23641074
11. Block of Synaptobrevin Inhibits Endocytosis Induced by boiled tetanus toxin. PMID: 23643538
12. SNAP23-VAMP2 interaction plays a key role in cAMP-mediated exocytosis from parotid glands. PMID: 23380067
13. Amyloid-beta acts as a regulator of neurotransmitter release disrupting the interaction between synaptophysin and VAMP2 PMID: 22905234
14. a mechanism whereby fusion pore formation is induced by movement of the charged syb2 C-terminus within the membrane in response to pulling and tilting force PMID: 23009845
15. VAMP2, SNAP25b and syntaxin 1 characterize most cerebellar glutamatergic synapses and only one type of GABAergic synapse. PMID: 22094010
16. Dysregulation of SNARE complex and syt-1 in prefrontal cortex of adult-onset hypothyroidism can be restored by T(4) treatment. PMID: 21646859
17. Munc18-1 and the neuronal SNAREs (t-SNARE (syntaxin 1.SNAP-25) and v-/t-SNARE (VAMP2.syntaxin 1.SNAP-25) complexes) already have the inherent capability to function as a basic stage-specific off/on switch to control membrane fusion PMID: 21730064
18. Data show that most of the synaptobrevin SNARE motif has a remarkable reluctance to bind membranes. PMID: 21768342
19. Synaptophysin and synaptobrevin 2 were expressed in a dynamic manner during the development of rat cochlea PMID: 21556117
20. Data showv that complexin 2 interacts with vesicle-associated membrane protein (VAMP) 2, syntaxins 3 and 4. PMID: 20829354
21. In the incisor dental pulp, all nerve fibers display immunoreactivity for syntaxin-1, synaptosomal-associated protein (SNAP)-25, and vesicle-associated membrane protein (VAMP)-2. PMID: 20186959
22. the ability of sybII to support exocytosis is inhibited by addition of one or two residues to the sybII C terminus depending on their energy of transfer from water to the membrane interface, following a Boltzmann distribution PMID: 20937897
23. tomosyn controls synaptic vesicle fusion positively by serving as a placeholder for VAMP2. PMID: 20633536
24. Recombinant VAMP2 could serve as a replacement for VAMP2 synthetic peptide, potentially useful in endopeptidase assays for replacement of the currently used mouse bioassay for clostridial neurotoxins contaminating biotherapeutic products. PMID: 20005125
25. synaptobrevin 2 forms complexes with the plasma membrane-bound SNAREs syntaxin 1A and SNAP25 to initiate the fusion reaction. PMID: 12177041
26. Data suggest that synaptophysin I has multiple roles in neurotransmitter release, regulating VAMP2 availability for the soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex and participating in the late steps of exocytosis. PMID: 12181340
27. VAMP2 mRNA is increased during nerve regeneration of the facial motor nucleus after axotomy. PMID: 12191731
28. Dimerization of synaptobrevin 2 in membranes is very weak, questioning any possible functional role for this association in vivo. PMID: 12501216
29. vesicle-associated membrane protein 2 is involved in secretion of polypeptides from the choroid plexus epithelium. PMID: 12559091
30. cytoplasmic domain of VAMP2 was found to be necessary for both the formation of VAMP2-SypI hetero-dimers and for VAMP2 sorting to SVs PMID: 14528015
31. Synaptobrevin-2 is present in approximately 35% of the taste cells in rat circumvallate taste buds and colocalizes with SNAP-25, serotonin, protein gene product 9.5. and type III inositol 1,4,5-triphosphate receptor. PMID: 14983476
32. Homodimerization of Vamp2 is mediated by its transmembrane segment. PMID: 15109254
33. Data suggest that VAMP2-dependent exocytosis regulates plasma membrane insertion of TRPC3 channels and contributes to carbachol-stimulation of Ca2+ influx. PMID: 15327778
34. cAMP increases NKCC2 surface expression by a mechanism involving VAMP and that NKCC2 trafficking to the apical membrane is involved in the stimulation of Tkidney medulla NaCl absorption by cAMP. PMID: 16144963
35. VAMP 2 is the most abundant isoform in the rat brain and is widely distributed PMID: 16169186
36. in astrocytes, a subpopulation of vesicles (tagged with a synaptobrevin2-EGFP chimera) is highly mobile and can fuse with the plasma membrane, at the level of the astrocyte processes, in a Ca2+-dependent manner PMID: 16322057
37. results show SNARE nucleation restricted to N-terminal portion; zippering proceeds in an N- to C-terminal direction; synaptobrevin binds rapidly to syntaxin/SNAP-25 acceptor; stabilizing syntaxin/SNAP-25 acceptor by a peptide allowed fast liposome fusion PMID: 16888141
38. Individual pancreatic acinar cells express VAMP 2-specific populations of zymogen granules that orchestrate the constitutive and calcium(2+)-regulated secretory pathways. PMID: 17272274
39. VAMP2 is expressed in muscle satellite cells and up-regulated during muscle regeneration. PMID: 17468895
40. Cleavage of synaptobrevin 2 by tetanus toxin, known to reduce neurotransmission, did not affect the respiratory response to K+, whereas the general excitability of d PC12 cells increased PMID: 18086678
41. analysis of SNARE mutations that cause a decrease in the ability of botulinum toxin-resistant synaptobrevin 2 to rescue regulated exocytosis in toxin-treated neuroendocrine cells PMID: 18508917
42. analysis of the substrate recognition mechanism of VAMP/synaptobrevin-cleaving clostridial neurotoxins PMID: 18511418
43. VAMP2 may contribute to the activity dependence of dense-core vesicles release PMID: 18542995
44. Findings suggest the involvement of VAMP2 in the development of skeletal muscles of somitic and non-somitic origins. PMID: 18570252
45. Results show that synaptophysin-containing cells co-expressed vesicular-associated membrane protein 2 and cholecystokinin. PMID: 19253017
46. 30 mW/cm(2) (SAR 14.1 W/kg) microwave radiation can result in the perturbation of the synaptic vesicles associated proteins: synapsin I, synaptophysin, VAMP-2, and syntaxin. PMID: 19603498
47. VAMP2, VAMP5, and VAMP7 may be involved in translocation of GLUT4 during muscle contractions. PMID: 19675279
48. Data suggest that VAMP2 modulates Kv2.1 inactivation by interfering with the interaction between the docking loop and C1a, a mechanism for gating regulation that may pertain also to other Kv channels. PMID: 19690160
49. Under appropriate conditions a docked state, mediated by trans-SNARE interactions, can be isolated that constitutes an intermediate in the fusion pathway. PMID: 19843696

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KEGG: rno:24803

STRING: 10116.ENSRNOP00000054114

UniGene: Rn.12939