The Vesicle-associated membrane protein 2 encoded by VAMP2 gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. VAMP2 is a key part of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) that is involved in synaptic vesicle exocytosis, a fundamental step in neurotransmitter release between docking and fusion. The protein forms a stable complex with syntaxin, synaptosomal-associated protein, and synaptotagmin. It also forms a distinct complex with synaptophysin. Besides, VAMP2 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1.
|Basic Information of VAMP2|
|Protein Name||Vesicle-associated membrane protein 2 (VAMP-2)|
|Organism||Homo sapiens (Human)|
VAMP2 plays a crucial role in membrane fusion, mediating protein trafficking and the secretion of physiological mediators. Except that, the VAMP2 plays vital roles in other processes. VAMP2 can function as a molecular marker for both quiescent satellite cells and myotubes, but not for proliferating myoblasts. Thyroid hormone may promote glucose uptake via enhancing insulin-induced phosphorylation of Akt and subsequent translocations of VAMP2 and GLUT4 in 3T3-L1 adipocytes. Additionally, by reducing VAMP2 expression in a murine model of epilepsy, mice showed significant reductions in potassium-evoked glutamate release, which leads to a kindling-resistant phenotype. Because VAMP2 gene encodes a synaptic vesicle protein and its special map location, it may play role in the pathogenesis of Familial Infantile Myasthenia Gravis (FIMG).
Fig.1 A model for tethering and fusion of Tfn-TfnR-containing recycling vesicles with the PM, mediated by Rab11, the exocyst and SNAREs. (Kubo, 2015)
This article finds that cAMP stimulation enhances VAMP2 exocytosis and promotes VAMP2 interaction with NKCC2.
This article suggests that VAMP2-NRG1 fusion gene, in particular, its most dominant splice variant, is capable of promoting cellular growth and thus likely functions as an oncogene.
This article suggests that the distribution of SNAP25, VAMP1 and VAMP2 is age-related and submitted to estrogenic control during development. Changes in SNAP25, VAMP1 and VAMP2 in defined nerve terminals could correlate with alterations of specific synaptic properties.
This article reveals an essential role for AP180-mediated high-fidelity sorting of Syb2 in SV reformation and neurotransmission.
This article suggests that the Aβ-miR-34cVAMP2 pathway partially explains the mechanism underlying VAMP2 reduction in AD patients.
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