Biology:VAMP2

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example


Hypothetic models of VAMP2 conformations and engagement in SNARE complex assembly for neurotransmitter release

Vesicle-associated membrane protein 2 (VAMP2) is a protein that in humans is encoded by the VAMP2 gene.[1][2]

Function

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. VAMP2 is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. VAMP2 is thought to participate in neurotransmitter release at a step between docking and fusion. Mice lacking functional synaptobrevin2/VAMP2 gene cannot survive after birth, and have a dramatically reduced synaptic transmission, around 10% of control.[3] The protein forms a stable complex with syntaxin, synaptosomal-associated protein, 25 kD, and complexin. It also forms a distinct complex with synaptophysin.[2]

Clinical significance

Heterozygous mutations in VAMP2 cause a neurodevelopmental disorder with hypotonia and autistic features (with or without hyperkinetic movements).[4][5][6]

Interactions

VAMP2 has been shown to interact with:


References

  1. ↑ "Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2". The Journal of Biological Chemistry 265 (28): 17267–73. Oct 1990. doi:10.1016/S0021-9258(17)44898-8. PMID 1976629. 
  2. ↑ 2.0 2.1 "Entrez Gene: VAMP2 vesicle-associated membrane protein 2 (synaptobrevin 2)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6844. 
  3. ↑ "SNARE function analyzed in synaptobrevin/VAMP knockout mice". Science 294 (5544): 1117–22. Nov 2001. doi:10.1126/science.1064335. PMID 11691998. Bibcode: 2001Sci...294.1117S. 
  4. ↑ "Mutations in the Neuronal Vesicular SNARE VAMP2 Affect Synaptic Membrane Fusion and Impair Human Neurodevelopment". The American Journal of Human Genetics 104 (4): 721‐730. Apr 2019. doi:10.1016/j.ajhg.2019.02.016. PMID 30929742. 
  5. ↑ "Variant in the neuronal vesicular SNARE VAMP2 (synaptobrevin-2): First report in Japan". Brain and Development 42 (7): 529–533. Apr 2020. doi:10.1016/j.braindev.2020.04.001. PMID 32336483. 
  6. ↑ "OMIM entry: Neurodevelopmental disorder with hypotonia and autistic features with or without hyperkinetic movements". https://www.omim.org/entry/618760. 
  7. ↑ "Isolation and characterization of a dual prenylated Rab and VAMP2 receptor". The Journal of Biological Chemistry 272 (43): 26991–8. Oct 1997. doi:10.1074/jbc.272.43.26991. PMID 9341137. 
  8. ↑ "Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis". The Journal of Biological Chemistry 276 (44): 40824–33. Nov 2001. doi:10.1074/jbc.M106141200. PMID 11524423. 
  9. ↑ 9.0 9.1 "Effect of mutations in vesicle-associated membrane protein (VAMP) on the assembly of multimeric protein complexes". The Journal of Neuroscience 17 (5): 1596–603. Mar 1997. doi:10.1523/JNEUROSCI.17-05-01596.1997. PMID 9030619. 
  10. ↑ 10.0 10.1 "Three-dimensional structure of the complexin/SNARE complex". Neuron 33 (3): 397–409. Jan 2002. doi:10.1016/s0896-6273(02)00583-4. PMID 11832227. https://epublications.marquette.edu/cgi/viewcontent.cgi?article=1227&context=chem_fac. 
  11. ↑ 11.0 11.1 "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". Journal of Immunology 164 (11): 5850–7. Jun 2000. doi:10.4049/jimmunol.164.11.5850. PMID 10820264. 
  12. ↑ "Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane". Archives of Oral Biology 48 (8): 597–604. Aug 2003. doi:10.1016/s0003-9969(03)00116-x. PMID 12828989. 
  13. ↑ "Role of SNAP23 in insulin-induced translocation of GLUT4 in 3T3-L1 adipocytes. Mediation of complex formation between syntaxin4 and VAMP2". The Journal of Biological Chemistry 275 (11): 8240–7. Mar 2000. doi:10.1074/jbc.275.11.8240. PMID 10713150. 
  14. ↑ "A conformational switch in syntaxin during exocytosis: role of munc18". The EMBO Journal 18 (16): 4372–82. Aug 1999. doi:10.1093/emboj/18.16.4372. PMID 10449403. 
  15. ↑ "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell 83 (1): 111–9. Oct 1995. doi:10.1016/0092-8674(95)90239-2. PMID 7553862. 
  16. ↑ "Munc 18a binding to syntaxin 1A and 1B isoforms defines its localization at the plasma membrane and blocks SNARE assembly in a three-hybrid system assay". Molecular and Cellular Neurosciences 20 (2): 169–80. Jun 2002. doi:10.1006/mcne.2002.1122. PMID 12093152. 
  17. ↑ "A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains". FEBS Letters 446 (1): 40–4. Mar 1999. doi:10.1016/s0014-5793(99)00028-9. PMID 10100611. 
  18. ↑ "Role of vesicle-associated membrane protein-2, through Q-soluble N-ethylmaleimide-sensitive factor attachment protein receptor/R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor interaction, in the exocytosis of specific and tertiary granules of human neutrophils". Journal of Immunology 170 (2): 1034–42. Jan 2003. doi:10.4049/jimmunol.170.2.1034. PMID 12517971. 
  19. ↑ "Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2". The Biochemical Journal. 317 317 (3): 945–54. Aug 1996. doi:10.1042/bj3170945. PMID 8760387. 
  20. ↑ "Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: implications for platelet secretion". Blood 93 (8): 2617–26. Apr 1999. doi:10.1182/blood.V93.8.2617. PMID 10194441. 

Further reading




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