VAMP2

VAMP2
Estruturas dispoñibles
PDB	Buscar ortólogos: PDBe, RCSB  Lista de códigos PDB 3FIE, 3FII, 3RK2, 3RK3, 3RL0
Identificadores
Nomenclatura	Outros nomes VAMP2, SYB2, VAMP-2, proteína de membrana asociada a vesículas 2, NEDHAHM
Símbolo	VAMP2 (HGNC: 12643)
Identificadores externos	OMIM: 185881 MGI: 1313277 HomoloGene: 7591 EBI: VAMP2 GeneCards: Xene VAMP2 UniProt: VAMP2
Locus	Cr. 17 p13.1
Ontoloxía Xénica Referencias: AmiGO / QuickGO
Padrón de expresión de ARNm
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

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

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

A VAMP2 presenta interaccións con:

• RABAC1,^[4]
• SNAP-25,^[5][6][7]
• SNAP23,^[8][9][10]
• STX1A,^{[6][7][11][12][13][14]} e
• STX4.^{[8][15][16][17]}

Notas

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. "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. 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. 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. 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

Bibliografía

• Brumell JH, Volchuk A, Sengelov H, Borregaard N, Cieutat AM, Bainton DF, Grinstein S, Klip A (Dec 1995). "Subcellular distribution of docking/fusion proteins in neutrophils, secretory cells with multiple exocytic compartments". Journal of Immunology 155 (12): 5750–9. PMID 7499863. 
• Kutay U, Ahnert-Hilger G, Hartmann E, Wiedenmann B, Rapoport TA (Jan 1995). "Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane". The EMBO Journal 14 (2): 217–23. PMC 398073. PMID 7835332. 
• Chapman ER, An S, Barton N, Jahn R (Nov 1994). "SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils". The Journal of Biological Chemistry 269 (44): 27427–32. PMID 7961655. 
• Hunt JM, Bommert K, Charlton MP, Kistner A, Habermann E, Augustine GJ, Betz H (Jun 1994). "A post-docking role for synaptobrevin in synaptic vesicle fusion". Neuron 12 (6): 1269–79. PMID 8011337. doi:10.1016/0896-6273(94)90443-X. 
• Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. PMID 8125298. doi:10.1016/0378-1119(94)90802-8. 
• 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. 
• Mandon B, Chou CL, Nielsen S, Knepper MA (Aug 1996). "Syntaxin-4 is localized to the apical plasma membrane of rat renal collecting duct cells: possible role in aquaporin-2 trafficking". The Journal of Clinical Investigation 98 (4): 906–13. PMC 507504. PMID 8770861. doi:10.1172/JCI118873. 
• Timmers KI, Clark AE, Omatsu-Kanbe M, Whiteheart SW, Bennett MK, Holman GD, Cushman SW (Dec 1996). "Identification of SNAP receptors in rat adipose cell membrane fractions and in SNARE complexes co-immunoprecipitated with epitope-tagged N-ethylmaleimide-sensitive fusion protein". The Biochemical Journal. 320 320 (2): 429–36. PMC 1217948. PMID 8973549. doi:10.1042/bj3200429. 
• Betz A, Okamoto M, Benseler F, Brose N (Jan 1997). "Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin". The Journal of Biological Chemistry 272 (4): 2520–6. PMID 8999968. doi:10.1074/jbc.272.4.2520. 
• 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. 
• 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. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. PMID 9373149. doi:10.1016/S0378-1119(97)00411-3. 
• Weir ML, Klip A, Trimble WS (Jul 1998). "Identification of a human homologue of the vesicle-associated membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a broadly expressed protein that binds to VAMP". The Biochemical Journal. 333 333 (2): 247–51. PMC 1219579. PMID 9657962. doi:10.1042/bj3330247. 
• Isenmann S, Khew-Goodall Y, Gamble J, Vadas M, Wattenberg BW (Jul 1998). "A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal". Molecular Biology of the Cell 9 (7): 1649–60. PMC 25402. PMID 9658161. doi:10.1091/mbc.9.7.1649. 
• Prekeris R, Klumperman J, Chen YA, Scheller RH (Nov 1998). "Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes". The Journal of Cell Biology 143 (4): 957–71. PMC 2132958. PMID 9817754. doi:10.1083/jcb.143.4.957. 
• Nishimura Y, Hayashi M, Inada H, Tanaka T (Jan 1999). "Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins". Biochemical and Biophysical Research Communications 254 (1): 21–6. PMID 9920726. doi:10.1006/bbrc.1998.9876. 
• Valdez AC, Cabaniols JP, Brown MJ, Roche PA (Mar 1999). "Syntaxin 11 is associated with SNAP-23 on late endosomes and the trans-Golgi network". Journal of Cell Science. 112 112 (6): 845–54. PMID 10036234. 
• 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. 
• Fasshauer D, Antonin W, Margittai M, Pabst S, Jahn R (May 1999). "Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties". The Journal of Biological Chemistry 274 (22): 15440–6. PMID 10336434. doi:10.1074/jbc.274.22.15440.