Vesicle-associated membrane protein 8 encoded by VAMP8 gene was first identified as an endosomal SNARE. SNARE is recruited to mature autophagosomes where it forms a complex with endolysosomal VAMP8 and cytoplasmic synaptosomal-associated protein (SNAPs). SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. VAMP8 has been revealed to participate in biological functions like endosomal fusion, the exocytosis of GLUT4 and insulin, sequential granule-to-granule fusion and autophagy.
|Basic Information of VAMP8|
|Protein Name||Vesicle-associated membrane protein 81 Publication (VAMP-8)|
|Organism||Homo sapiens (Human)|
VAMP8 found in endo-lysosomes is involved in endosome-lysosome fusion or autophagosome-lysosome fusion via its interaction with the STX17-SNAP29 binary t-SNARE complex. VAMP8 is involved in dense-granule secretion. The involvement of both VAMP8 in dense-granule fusion may be related to the fact that platelet exocytosis proceeds through compound fusion between α and dense granules and the plasma membrane. VAMP8 is enriched in the membrane of pancreatic zymogen granules and is necessary for regulated secretion in response to secretagogues as well as for mis-fusion of zymogen granules with the basolateral membrane under supramaximal stimulus. VAMP8 might be a part of the machinery involved in the development of pancreatitis. VAMP8 involves the separation of the midbody during cell division, which leads to the complete separation of daughter cells. VAMP8 within other SNARE complex combinations is involved in homotypic late endosome and exocytotic fusion events.
Fig.1 SNARE-dependent fusion of platelet granules with the plasma membrane. Top panels depict α granules or dense granules (left) or lysosomes (right) in resting platelets. (Marks, 2012)
This article exemplified by VAMP8 finds the critical functions of SNAREs in tumor progression as well as chemosensitivity.
This article suggests that Sbf/MTMR13 and Rab21 GTPase activity regulates VAMP8 endosomal sorting to lysosomes in a demand-dependent fashion, serving as a novel mechanism for autophagy regulation.
This article suggests no significant association between the SNPs in VAMP8 gene region and glioma risk, indicating that these variants might not contribute to glioma susceptibility in the Chinese Han population.
This article reveals a role for VAMP8 in fusion of recycling endosomes with the plasma membrane.
This article suggests that VAMP8-/- in pancreatic acinar cells results in the enhanced expression and partial redistribution of TI-VAMP7, VAMP4, and Rab11a to ZGs and a compensatory increase in constitutive secretion.
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