VAMP2

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VAMP2
Protein VAMP2 PDB 1kil.png
Estruturas dispoñibles
PDBBuscar ortólogos: PDBe, RCSB
Identificadores
Nomenclatura
SímboloVAMP2 (HGNC: 12643)
Identificadores
externos
LocusCr. 17 p13.1
Padrón de expresión de ARNm
PBB GE VAMP2 201556 s at fs.png
PBB GE VAMP2 214792 x at fs.png
PBB GE VAMP2 201557 at fs.png
Máis información
Ortólogos
Especies
Humano Rato
Entrez
6844 22318
Ensembl
Véxase HS Véxase MM
UniProt
P63027 P63044
RefSeq
(ARNm)
NM_014232 NM_009497
RefSeq
(proteína) NCBI
NP_001317054 NP_033523
Localización (UCSC)
Cr. 17:
8.16 – 8.16 Mb
Cr. 11:
69.09 – 69.09 Mb
PubMed (Busca)
6844


22318
Modelos hipotéticos de conformacións de VAMP2 e intervención na ensamblaxe do complexo SNARE para a liberación de neurotransmisores

A proteína de membrana asociada a vesículas 2 (ou VAMP2, do inglés Vesicle-associated membrane protein 2) é unha proteína que nos humanos está codificada polo xene VAMP2 do cromosoma 17.[1][2]

Función[editar | editar a fonte]

As sinaptobrevinas/VAMPs, sintaxinas e a proteína asociada ao sinaptosoma de 25 kD SNAP25 son os principais compoñentes dun complexo proteico implicado no atraque e/ou fusión de vesículas sinápticas coa membrana presináptica. A VAMP2 é un membro da familia da proteína de membrana asociada a vesículas (VAMP)/sinaptobrevina. Crese que a VAMP2 participa na liberación de neurotransmisores nun paso entre o atraque e a fusión. Os ratos que carecen dun xene funcional sinaptobrevina2/VAMP2 non poden sobrevivir despois do nacemento, e teñen unha transmisión sináptica drasticamente reducida, arredor do 10% do control.[3] A proteína forma un complexo estable coa sintaxina, a SNAP25, e a complexina. Tamén forma un complexo diferente coa sinaptofisina.[2]

Importancia clínica[editar | editar a fonte]

A VAMP2 é un probable xene candidato causante da miastenia infantil familiar debido ao seu mapa de localización e porque codifica unha proteína das vesículas sinápticas do tipo da que foi implicada na patoxénese de dita miastenia.

Interaccións[editar | editar a fonte]

A VAMP2 presenta interaccións con:

Notas[editar | editar a fonte]

  1. Archer BT, Ozçelik T, Jahn R, Francke U, Südhof TC (Oct 1990). "Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2". The Journal of Biological Chemistry 265 (28): 17267–73. PMID 1976629. 
  2. 2,0 2,1 "Entrez Gene: VAMP2 vesicle-associated membrane protein 2 (synaptobrevin 2)". 
  3. Schoch S, Deák F, Königstorfer A, Mozhayeva M, Sara Y, Südhof TC, Kavalali ET (Nov 2001). "SNARE function analyzed in synaptobrevin/VAMP knockout mice". Science 294 (5544): 1117–22. Bibcode:2001Sci...294.1117S. PMID 11691998. doi:10.1126/science.1064335. 
  4. Martincic I, Peralta ME, Ngsee JK (Oct 1997). "Isolation and characterization of a dual prenylated Rab and VAMP2 receptor". The Journal of Biological Chemistry 272 (43): 26991–8. PMID 9341137. doi:10.1074/jbc.272.43.26991. 
  5. Li Y, Chin LS, Weigel C, Li L (Nov 2001). "Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis". The Journal of Biological Chemistry 276 (44): 40824–33. PMID 11524423. doi:10.1074/jbc.M106141200. 
  6. 6,0 6,1 Hao JC, Salem N, Peng XR, Kelly RB, Bennett MK (Mar 1997). "Effect of mutations in vesicle-associated membrane protein (VAMP) on the assembly of multimeric protein complexes". The Journal of Neuroscience 17 (5): 1596–603. PMC 6573372. PMID 9030619. doi:10.1523/JNEUROSCI.17-05-01596.1997. 
  7. 7,0 7,1 Chen X, Tomchick DR, Kovrigin E, Araç D, Machius M, Südhof TC, Rizo J (Jan 2002). "Three-dimensional structure of the complexin/SNARE complex". Neuron 33 (3): 397–409. PMID 11832227. doi:10.1016/s0896-6273(02)00583-4. 
  8. 8,0 8,1 Paumet F, Le Mao J, Martin S, Galli T, David B, Blank U, Roa M (Jun 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". Journal of Immunology 164 (11): 5850–7. PMID 10820264. doi:10.4049/jimmunol.164.11.5850. 
  9. Imai A, Nashida T, Yoshie S, Shimomura H (Aug 2003). "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. PMID 12828989. doi:10.1016/s0003-9969(03)00116-x. 
  10. Kawanishi M, Tamori Y, Okazawa H, Araki S, Shinoda H, Kasuga M (Mar 2000). "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. PMID 10713150. doi:10.1074/jbc.275.11.8240. 
  11. Dulubova I, Sugita S, Hill S, Hosaka M, Fernandez I, Südhof TC, Rizo J (Aug 1999). "A conformational switch in syntaxin during exocytosis: role of munc18". The EMBO Journal 18 (16): 4372–82. PMC 1171512. PMID 10449403. doi:10.1093/emboj/18.16.4372. 
  12. McMahon HT, Missler M, Li C, Südhof TC (Oct 1995). "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell 83 (1): 111–9. PMID 7553862. doi:10.1016/0092-8674(95)90239-2. 
  13. Pérez-Brangulí F, Muhaisen A, Blasi J (Jun 2002). "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. PMID 12093152. doi:10.1006/mcne.2002.1122. 
  14. Margittai M, Otto H, Jahn R (Mar 1999). "A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains". FEBS Letters 446 (1): 40–4. PMID 10100611. doi:10.1016/s0014-5793(99)00028-9. 
  15. Mollinedo F, Martín-Martín B, Calafat J, Nabokina SM, Lazo PA (Jan 2003). "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. PMID 12517971. doi:10.4049/jimmunol.170.2.1034. 
  16. Jagadish MN, Fernandez CS, Hewish DR, Macaulay SL, Gough KH, Grusovin J, Verkuylen A, Cosgrove L, Alafaci A, Frenkel MJ, Ward CW (Aug 1996). "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. PMC 1217577. PMID 8760387. doi:10.1042/bj3170945. 
  17. Reed GL, Houng AK, Fitzgerald ML (Apr 1999). "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. PMID 10194441. doi:10.1182/blood.V93.8.2617. 

Véxase tamén[editar | editar a fonte]

Bibliografía[editar | editar a fonte]