Vesicle-associated membrane protein 8 is a
protein that in humans is encoded by the VAMP8gene.[5][6][7]
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. The protein encoded by this gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. It is associated with the perinuclear vesicular structures of the early endocytic compartment. It has been found that VAMP8 interacts specifically with the soluble NSF-attachment protein (alpha-SNAP), most likely through an VAMP8-containing SNARE complex.[7] Phosphorylation of VAMP8 inside the conserved SNARE-domain can suppress vesicle fusion.[8]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Bui TD, Wong SH, Lu L, Hong W (February 1999). "Endobrevin maps to chromosome 2 in human and chromosome 6 in mouse". Genomics. 54 (3): 579–80.
doi:
10.1006/geno.1998.5596.
PMID9878266.
^Polgár J, Chung Sul-Hee, Reed Guy L (August 2002). "Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion". Blood. 100 (3): 1081–3.
doi:
10.1182/blood.V100.3.1081.
ISSN0006-4971.
PMID12130530.
S2CID36597939.
^Imai A, Nashida Tomoko, Yoshie Sumio, Shimomura Hiromi (August 2003). "Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane". Arch. Oral Biol. 48 (8): 597–604.
doi:
10.1016/S0003-9969(03)00116-X.
ISSN0003-9969.
PMID12828989.
^Nagamatsu S, Nakamichi Y, Watanabe T, Matsushima S, Yamaguchi S, Ni J, Itagaki E, Ishida H (January 2001). "Localization of cellubrevin-related peptide, endobrevin, in the early endosome in pancreatic beta cells and its physiological function in exo-endocytosis of secretory granules". J. Cell Sci. 114 (Pt 1): 219–227.
doi:
10.1242/jcs.114.1.219.
ISSN0021-9533.
PMID11112705.
Nagamatsu S, Nakamichi Y, Watanabe T, et al. (2001). "Localization of cellubrevin-related peptide, endobrevin, in the early endosome in pancreatic beta cells and its physiological function in exo-endocytosis of secretory granules". J. Cell Sci. 114 (Pt 1): 219–227.
doi:
10.1242/jcs.114.1.219.
PMID11112705.
Polgár J, Chung SH, Reed GL (2002). "Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion". Blood. 100 (3): 1081–3.
doi:
10.1182/blood.V100.3.1081.
PMID12130530.
S2CID36597939.
Imai A, Nashida T, Yoshie S, Shimomura H (2003). "Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane". Arch. Oral Biol. 48 (8): 597–604.
doi:
10.1016/S0003-9969(03)00116-X.
PMID12828989.
Brinkman JF, Ottenheim CP, de Jong LA, et al. (2006). "VAMP5 and VAMP8 are most likely not involved in primary open-angle glaucoma". Mol. Vis. 11: 582–6.
PMID16110299.
Oishi Y, Arakawa T, Tanimura A, et al. (2007). "Role of VAMP-2, VAMP-7, and VAMP-8 in constitutive exocytosis from HSY cells". Histochem. Cell Biol. 125 (3): 273–81.
doi:
10.1007/s00418-005-0068-y.
PMID16195891.
S2CID10541252.
Vesicle-associated membrane protein 8 is a
protein that in humans is encoded by the VAMP8gene.[5][6][7]
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. The protein encoded by this gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. It is associated with the perinuclear vesicular structures of the early endocytic compartment. It has been found that VAMP8 interacts specifically with the soluble NSF-attachment protein (alpha-SNAP), most likely through an VAMP8-containing SNARE complex.[7] Phosphorylation of VAMP8 inside the conserved SNARE-domain can suppress vesicle fusion.[8]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Bui TD, Wong SH, Lu L, Hong W (February 1999). "Endobrevin maps to chromosome 2 in human and chromosome 6 in mouse". Genomics. 54 (3): 579–80.
doi:
10.1006/geno.1998.5596.
PMID9878266.
^Polgár J, Chung Sul-Hee, Reed Guy L (August 2002). "Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion". Blood. 100 (3): 1081–3.
doi:
10.1182/blood.V100.3.1081.
ISSN0006-4971.
PMID12130530.
S2CID36597939.
^Imai A, Nashida Tomoko, Yoshie Sumio, Shimomura Hiromi (August 2003). "Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane". Arch. Oral Biol. 48 (8): 597–604.
doi:
10.1016/S0003-9969(03)00116-X.
ISSN0003-9969.
PMID12828989.
^Nagamatsu S, Nakamichi Y, Watanabe T, Matsushima S, Yamaguchi S, Ni J, Itagaki E, Ishida H (January 2001). "Localization of cellubrevin-related peptide, endobrevin, in the early endosome in pancreatic beta cells and its physiological function in exo-endocytosis of secretory granules". J. Cell Sci. 114 (Pt 1): 219–227.
doi:
10.1242/jcs.114.1.219.
ISSN0021-9533.
PMID11112705.
Nagamatsu S, Nakamichi Y, Watanabe T, et al. (2001). "Localization of cellubrevin-related peptide, endobrevin, in the early endosome in pancreatic beta cells and its physiological function in exo-endocytosis of secretory granules". J. Cell Sci. 114 (Pt 1): 219–227.
doi:
10.1242/jcs.114.1.219.
PMID11112705.
Polgár J, Chung SH, Reed GL (2002). "Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion". Blood. 100 (3): 1081–3.
doi:
10.1182/blood.V100.3.1081.
PMID12130530.
S2CID36597939.
Imai A, Nashida T, Yoshie S, Shimomura H (2003). "Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane". Arch. Oral Biol. 48 (8): 597–604.
doi:
10.1016/S0003-9969(03)00116-X.
PMID12828989.
Brinkman JF, Ottenheim CP, de Jong LA, et al. (2006). "VAMP5 and VAMP8 are most likely not involved in primary open-angle glaucoma". Mol. Vis. 11: 582–6.
PMID16110299.
Oishi Y, Arakawa T, Tanimura A, et al. (2007). "Role of VAMP-2, VAMP-7, and VAMP-8 in constitutive exocytosis from HSY cells". Histochem. Cell Biol. 125 (3): 273–81.
doi:
10.1007/s00418-005-0068-y.
PMID16195891.
S2CID10541252.