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VAMP8 Membrane Protein Introduction

Introduction of VAMP8

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)
Gene Name VAMP8
Aliases Endobrevin (EDB)
Organism Homo sapiens (Human)
UniProt ID Q9BV40
Transmembrane Times 1
Length (aa) 100
Sequence MEEASEGGGNDRVRNLQSEVEGVKNIMTQNVERILARGENLEHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVLICVIVFIIILFIVLFATGAFS

Function of VAMP8 Membrane Protein

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.

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. 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)

Application of VAMP8 Membrane Protein in Literature

  1. Chen Y., et al. VAMP8 facilitates cellular proliferation and temozolomide resistance in human glioma cells. Neuro Oncology. 2015, 17(3):407-18. PubMed ID: 25209430

    This article exemplified by VAMP8 finds the critical functions of SNAREs in tumor progression as well as chemosensitivity.

  2. Jean S., et al. Starvation-induced MTMR13 and RAB21 activity regulates VAMP8 to promote autophagosome-lysosome fusion. EMBO Rep. 2015, 16(3):297-311. PubMed ID: 25648148

    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.

  3. Zhou P., et al. No association of VAMP8 gene polymorphisms with glioma in a Chinese Han population. Int J Clin Exp Pathol. 2015, 8(5):5681-7. PubMed ID: 26191281

    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.

  4. Marshall M.R., et al. VAMP8-dependent fusion of recycling endosomes with the plasma membrane facilitates T lymphocyte cytotoxicity. Journal of Cell Biology. 2015, 210(1):135-51. PubMed ID: 26124288

    This article reveals a role for VAMP8 in fusion of recycling endosomes with the plasma membrane.

  5. Messenger S.W., et al. Vesicle associated membrane protein 8 (VAMP8)-mediated zymogen granule exocytosis is dependent on endosomal trafficking via the constitutive-like secretory pathway. Journal of Biological Chemistry. 2014, 289(40):28040-53. PubMed ID: 25138214

    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.

VAMP8 Preparation Options

Membrane protein studies have advanced significantly over the past few years. Based on our versatile Magic™ membrane protein production platform, we could offer a series of membrane protein preparation services for worldwide customers in reconstitution forms as well as multiple active formats. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-VAMP8 antibody development services.


During the past years, Creative Biolabs has successfully generated many functional membrane proteins for our global customers. We are happy to accelerate the development of our clients’ programs with our one-stop, custom-oriented service. For more detailed information, please feel free to contact us.

Reference

  1. Marks M S. (2012). SNARing platelet granule secretion. Blood. 120(12): 2355-7.

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