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findings reveal a novel signalling pathway involved in development of the semicircular canal system, and suggest a previously unrecognized role for NCS-1 (show NCS1 Proteins) in mitochondrial function via its association with several mitochondrial proteins.
These observations provide evidence that the synaptobrevin-2 transmembrane domain catalyzes the membrane fusion process by its structural flexibility, actively setting the pace of fusion pore expansion.
Syp1 (show SYP Proteins) clears Syb2 from the presynaptic active zone to prevent short-term depression.
The balance between synaptophysin (show SYP Proteins) and sybII levels is critical for the correct targeting of sybII to synaptic vesicles and suggests that alterations in synaptophysin (show SYP Proteins) levels might affect the localisation of sybII and subsequent presynaptic performance.
Thus, lipid-anchored syb2 provides little or no support for exocytosis, and anchoring syb2 to a membrane by a TMD (show TTN Proteins) greatly improves its function
Vamp2 mutations impair the ability of Munc18-1 (show STXBP1 Proteins) to promote trans-SNARE (show VTI1B Proteins) zippering. These mutations inhibit spontaneous as well as evoked neurotransmitter release, providing evidence for the Vamp2-regulating function of Munc18-1 (show STXBP1 Proteins) in synaptic exocytosis.
These results provide a novel molecular mechanism for autocrine negative feedback regulation of insulin (show INS Proteins) secretion.
Results suggest that side chains in the syb2 transmembrane domain influence the kinetics of exocytosis by perturbing the packing of the surrounding lipids
we demonstrate that Syb2 and SNAP25 (show SNAP25 Proteins) mediate the vesicular release of BDNF (show BDNF Proteins) in axons and dendrites of cortical neurons
Here we report on transgenic mice expressing a ubiquitinated synaptic vesicle protein (Ub(G76V)-GFP-Syb2) that develop progressive degeneration of motor nerve terminals.
VAMP2 is the major v-SNARE (show GOSR1 Proteins) involved in GLUT4 (show SLC2A4 Proteins) trafficking to the surface of 3T3-L1 adipocytes.
Data suggest that A-syn (show FYN Proteins) (alpha-synuclein) promotes SNARE (show NAPA Proteins)-dependent vesicle docking; phosphatidylserine (PS) removal from t-SNARE (show NAPA Proteins)-bearing vesicles causes A-syn (show FYN Proteins) to inhibit vesicle docking; PS removal from v-SNARE (show VTI1B Proteins)-bearing vesicles promotes vesicle docking; the C-terminal 45 residues of A-syn (show FYN Proteins) are required for promotion of vesicle docking. (Here, t-SNARE (show NAPA Proteins) is SNAP-25 (show SNAP25 Proteins); v-SNARE (show VTI1B Proteins) is VAMP2.)
A significant interactive two-locus model of STX1A_rs4363087|VAMP2_rs2278637 (presynaptic genes) was observed among SVC (show COL4A1 Proteins) variants in all epilepsy cases.
VAMP2 is a promising new plasma cell marker
VAMP2 is involved in Porphyromonas gingivalis recycling pathway.VAMP2 is localized in early endosomes in gingival epithelial cells.
The present study addressed for the first time the unique substrate recognition mechanism of LC/F5 substrate cleavage of VAMP-2 by Botulinum Neurotoxin subtype F5.
This study showed that decreased Levels of VAMP2 correlate with Duration of Dementia.
VAMP2-NRG1 (show NRG1 Proteins) is a novel oncogenic fusion gene representing a new addition to the list of NRG1 (show NRG1 Proteins) fusion genes, which together may form an important diagnostic and clinical category of lung adenocarcinoma cases
A large vesicular pool of VAMP2 maintained by AP180 is crucial to sustain efficient neurotransmission.
SNARE (show NAPA Proteins) complex genes and their interactions may play a significant role in susceptibility and working memory of ADHD.
miR (show MLXIP Proteins)-206 regulates lung surfactant secretion by limiting the availability of VAMP-2 protein.
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.
VAMP2 is restricted from forming the SNARE (show NAPA Proteins) (soluble N-ethylmaleimide-sensitive fusion protein (show NSF Proteins) attachment protein receptor) complex in chromaffin granules from adrenal medullae to the same degree as in brain-purified synaptic vesicles.
Lengthening juxtamembrane region of synaptobrevin-2 severely reduced occurrence of rapid single events, leaving slow ones unchanged. It also impaired increase in fast-fusion mode that normally follows elevation of intracellular Ca2 (show CA2 Proteins)+ levels.
The protein encoded by this gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 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 thought to participate in neurotransmitter release at a step between docking and fusion. The protein forms a stable complex with syntaxin, synaptosomal-associated protein, 25 kD, and synaptotagmin. It also forms a distinct complex with synaptophysin. It is a likely candidate gene for familial infantile myasthenia (FIMG) because of its map location and because it encodes a synaptic vesicle protein of the type that has been implicated in the pathogenesis of FIMG.
vesicle-associated membrane protein 2 (synaptobrevin 2)
, synaptobrevin II
, vesicle-associated membrane 2
, Synaptobrevin 2 (vesicle-associated membrane protein VAMP-2)
, Vesicle-associated membrane protein (synaptobrevin 2)
, synaptobrevin 2
, vesicle associated membrane protein 2
, vesicle-associated membrane protein 2