Vesicle-associated membrane protein 8

Last updated
VAMP8
Protein VAMP8 PDB 1gl2.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases VAMP8 , EDB, VAMP-8, vesicle associated membrane protein 8
External IDs OMIM: 603177 MGI: 1336882 HomoloGene: 37846 GeneCards: VAMP8
Orthologs
SpeciesHumanMouse
Entrez

8673

22320

Ensembl

ENSG00000118640

ENSMUSG00000050732

UniProt

Q9BV40

O70404

RefSeq (mRNA)

NM_003761

NM_016794

RefSeq (protein)

NP_003752

NP_058074

Location (UCSC) Chr 2: 85.56 – 85.58 Mb Chr 6: 72.36 – 72.37 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Vesicle-associated membrane protein 8 is a protein that in humans is encoded by the VAMP8 gene. [5] [6] [7]

Contents

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]

Interactions

Vesicle-associated membrane protein 8 has been shown to interact with STX4, [9] [10] SNAP23, [9] [11] STX1A, [12] STX8 [13] and STX7. [13] [14]

Related Research Articles

<span class="mw-page-title-main">SNARE protein</span> Protein family

SNARE proteins – "SNAPREceptors" – are a large protein family consisting of at least 24 members in yeasts, more than 60 members in mammalian cells, and some numbers in plants. The primary role of SNARE proteins is to mediate the fusion of vesicles with the target membrane; this notably mediates exocytosis, but can also mediate the fusion of vesicles with membrane-bound compartments. The best studied SNAREs are those that mediate the release of synaptic vesicles containing neurotransmitters in neurons. These neuronal SNAREs are the targets of the neurotoxins responsible for botulism and tetanus produced by certain bacteria.

<span class="mw-page-title-main">Vesicle-associated membrane protein</span> Protein family

Vesicle associated membrane proteins (VAMPs) are a family of SNARE proteins with similar structure, and are mostly involved in vesicle fusion.

<span class="mw-page-title-main">Synaptobrevin</span>

Synaptobrevins are small integral membrane proteins of secretory vesicles with molecular weight of 18 kilodalton (kDa) that are part of the vesicle-associated membrane protein (VAMP) family.

<span class="mw-page-title-main">SNAP25</span> Protein-coding gene in the species Homo sapiens

Synaptosomal-Associated Protein, 25kDa (SNAP-25) is a Target Soluble NSF (N-ethylmaleimide-sensitive factor) Attachment Protein Receptor (t-SNARE) protein encoded by the SNAP25 gene found on chromosome 20p12.2 in humans. SNAP-25 is a component of the trans-SNARE complex, which accounts for membrane fusion specificity and directly executes fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together.

<span class="mw-page-title-main">CD59</span> Mammalian protein found in Homo sapiens

CD59 glycoprotein, also known as MAC-inhibitory protein (MAC-IP), membrane inhibitor of reactive lysis (MIRL), or protectin, is a protein that in humans is encoded by the CD59 gene. It is an LU domain and belongs to the LY6/uPAR/alpha-neurotoxin protein family.

<span class="mw-page-title-main">STX1A</span> Protein-coding gene in the species Homo sapiens

Syntaxin-1A is a protein that in humans is encoded by the STX1A gene.

<span class="mw-page-title-main">SNAP23</span> Protein-coding gene in the species Homo sapiens

Synaptosomal-associated protein 23 is a protein that in humans is encoded by the SNAP23 gene. Two alternative transcript variants encoding different protein isoforms have been described for this gene.

<span class="mw-page-title-main">VAMP2</span> Protein-coding gene in the species Homo sapiens

Vesicle-associated membrane protein 2 (VAMP2) is a protein that in humans is encoded by the VAMP2 gene.

<span class="mw-page-title-main">Vesicle-associated membrane protein 7</span> Protein-coding gene in the species Homo sapiens

Vesicle-associated membrane protein 7 (VAMP-7), is a protein that in humans is encoded by the VAMP7 gene also known as the or SYBL1 gene.

<span class="mw-page-title-main">STX7</span> Human protein and coding gene

Syntaxin-7 is a protein that in humans is encoded by the STX7 gene.

<span class="mw-page-title-main">STX6</span> Protein-coding gene in the species Homo sapiens

Syntaxin-6 is a protein that in humans is encoded by the STX6 gene.

<span class="mw-page-title-main">NAPA (gene)</span> Protein-coding gene in the species Homo sapiens

N-ethylmaleimide-sensitive factor Attachment Protein Alpha, also known as SNAP-α, is a SNAP protein that is involved in the intra-cellular trafficking and fusing of vesicles to target membranes in cells.

<span class="mw-page-title-main">VAMP3</span> Protein-coding gene in the species Homo sapiens

Vesicle-associated membrane protein 3 is a protein that in humans is encoded by the VAMP3 gene.

<span class="mw-page-title-main">STX8</span> Protein-coding gene in the species Homo sapiens

Syntaxin-8 is a protein that in humans is encoded by the STX8 gene. Syntaxin 8 directly interacts with HECTd3 and has similar subcellular localization. The protein has been shown to form the SNARE complex with syntaxin 7, vti1b and endobrevin. These function as the machinery for the homotypic fusion of late endosomes.

<span class="mw-page-title-main">VTI1B</span> Protein-coding gene in the species Homo sapiens

Vesicle transport through interaction with t-SNAREs homolog 1B is a protein that in humans is encoded by the VTI1B gene.

<span class="mw-page-title-main">RAB22A</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-22A is a protein that in humans is encoded by the RAB22A gene.

<span class="mw-page-title-main">Syntaxin 3</span> Protein-coding gene in the species Homo sapiens

Syntaxin 3, also known as STX3, is a protein which in humans is encoded by the STX3 gene.

Vesicle fusion is the merging of a vesicle with other vesicles or a part of a cell membrane. In the latter case, it is the end stage of secretion from secretory vesicles, where their contents are expelled from the cell through exocytosis. Vesicles can also fuse with other target cell compartments, such as a lysosome. Exocytosis occurs when secretory vesicles transiently dock and fuse at the base of cup-shaped structures at the cell plasma membrane called porosome, the universal secretory machinery in cells. Vesicle fusion may depend on SNARE proteins in the presence of increased intracellular calcium (Ca2+) concentration.

Munc-18 proteins are the mammalian homologue of UNC-18 and are a member of the Sec1/Munc18-like (SM) protein family. Munc-18 proteins have been identified as essential components of the synaptic vesicle fusion protein complex and are crucial for the regulated exocytosis of neurons and neuroendocrine cells.

<span class="mw-page-title-main">VTI1A</span> Protein-coding gene in the species Homo sapiens

Vesicle transport through interaction with t-SNAREs homolog 1A is a protein that in humans is encoded by the VTI1A gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000118640 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000050732 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ 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. PMID   9878266.
  6. ↑ Wong SH, Zhang T, Xu Y, Subramaniam VN, Griffiths G, Hong W (July 1998). "Endobrevin, a Novel Synaptobrevin/VAMP-Like Protein Preferentially Associated with the Early Endosome". Mol Biol Cell. 9 (6): 1549–63. doi:10.1091/mbc.9.6.1549. PMC   25382 . PMID   9614193.
  7. 1 2 "Entrez Gene: VAMP8 vesicle-associated membrane protein 8 (endobrevin)".
  8. ↑ Malmersjö S, Di Palma S, Diao J, Lai Y, Pfuetzner RA, Wang AL, McMahon MA, Hayer A, Porteus M, Bodenmiller B, Brunger AT, Meyer T (July 2016). "Phosphorylation of residues inside the SNARE complex suppresses secretory vesicle fusion". EMBO Journal. 35 (16): 1721–1843. doi:10.15252/embj.201694071. PMC   5010044 . PMID   27402227.
  9. 1 2 Paumet F, Le Mao J, Martin S, Galli T, David B, Blank U, Roa M (June 2000). "Soluble NSF attachment protein receptors (SNAREs) in RBL-2H3 mast cells: functional role of syntaxin 4 in exocytosis and identification of a vesicle-associated membrane protein 8-containing secretory compartment". J. Immunol. 164 (11): 5850–7. doi: 10.4049/jimmunol.164.11.5850 . ISSN   0022-1767. PMID   10820264.
  10. ↑ 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. ISSN   0006-4971. PMID   12130530. S2CID   36597939.
  11. ↑ 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. ISSN   0003-9969. PMID   12828989.
  12. ↑ 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. ISSN   0021-9533. PMID   11112705.
  13. 1 2 Antonin W, Holroyd C, Fasshauer D, Pabst S, Von Mollard G F, Jahn R (Dec 2000). "A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function". EMBO J. 19 (23): 6453–64. doi:10.1093/emboj/19.23.6453. ISSN   0261-4189. PMC   305878 . PMID   11101518.
  14. ↑ Wade N, Bryant N J, Connolly L M, Simpson R J, Luzio J P, Piper R C, James D E (June 2001). "Syntaxin 7 complexes with mouse Vps10p tail interactor 1b, syntaxin 6, vesicle-associated membrane protein (VAMP)8, and VAMP7 in b16 melanoma cells". J. Biol. Chem. 276 (23): 19820–7. doi: 10.1074/jbc.M010838200 . ISSN   0021-9258. PMID   11278762.

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