VAMP2

VAMP2
VAMP2
Protein VAMP2 PDB 1kil.png
사용 가능한 구조
PDBOrtholog 검색: PDBe RCSB
식별자
에일리어스VAMP2, SYB2, VAMP-2, 소포관련막단백질2, NEDHAHM
외부 IDOMIM : 185881 MGI : 1313277 HomoloGene : 7591 GenCard : VAMP2
맞춤법
종.인간마우스
엔트레즈
앙상블
유니프로트
RefSeq(mRNA)

NM_014232
NM_001330125

NM_009497

RefSeq(단백질)

NP_001317054
NP_055047

NP_033523

장소(UCSC)Chr 17: 8.16 ~8.16 MbChr 11: 68.98 ~68.98 Mb
PubMed 검색[3][4]
위키데이터
인간 보기/편집마우스 표시/편집
신경전달물질 방출을 위한 SNARE 복합조립체에서의 VAMP2 구성 및 결합 가설 모델

소포관련막단백질2(VAMP2)VAMP2유전자[5][6]의해 인간에게 암호화되는 단백질이다.

기능.

시냅토브레빈/VAMPs, 신트신 및 25-kD 시냅토솜 관련 단백질 SNAP25는 시냅스 전막과의 도킹 및/또는 융합에 관여하는 단백질 복합체의 주요 성분이다.VAMP2는 소포관련막단백질(VAMP)/시냅토브레빈 계열의 구성원이다.VAMP2는 도킹과 융합 사이의 단계에서 신경전달물질 방출에 관여하는 것으로 생각된다.기능성 시냅토브레빈2/VAMP2 유전자가 없는 생쥐는 출생 후 생존할 수 없으며 시냅스 전달이 극적으로 감소하여 [7]약 10%의 통제력을 가진다.단백질은 신트랜신, 시냅토좀 관련 단백질, 25kD 및 콤플렉신과 함께 안정적인 복합체를 형성한다.또한 시냅토피신[6]뚜렷한 콤플렉스를 형성합니다.

임상적 의의

VAMP2의 헤테로 접합 돌연변이는 저혈압과 자폐적 특징을 가진 신경 발달 장애를 일으킨다.[8][9][10]

상호 작용

VAMP2는 다음과 상호작용하는 으로 나타났습니다.

레퍼런스

  1. ^ a b c GRCh38: 앙상블 릴리즈 89: ENSG00000220205 - 앙상블, 2017년 5월
  2. ^ a b c GRCm38: 앙상블 릴리즈 89: ENSMUSG000020894 - 앙상블, 2017년 5월
  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. ^ 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.
  6. ^ a b "Entrez Gene: VAMP2 vesicle-associated membrane protein 2 (synaptobrevin 2)".
  7. ^ 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. doi:10.1126/science.1064335. PMID 11691998. S2CID 40321111.
  8. ^ Salpietro V, Malintan NT, Llano-Rivas I, et al. (Apr 2019). "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. doi:10.1016/j.ajhg.2019.02.016. PMC 6451933. PMID 30929742.
  9. ^ Sunaga Y, Muramatsu K, Kosaki K, et al. (Apr 2020). "Variant in the neuronal vesicular SNARE VAMP2 (synaptobrevin-2): First report in Japan". Brain and Development. 42 (7): 529–533. doi:10.1016/j.braindev.2020.04.001. PMID 32336483. S2CID 216095891.
  10. ^ "OMIM entry: Neurodevelopmental disorder with hypotonia and autistic features with or without hyperkinetic movements".
  11. ^ 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. doi:10.1074/jbc.272.43.26991. PMID 9341137.
  12. ^ 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. doi:10.1074/jbc.M106141200. PMID 11524423.
  13. ^ a b 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. doi:10.1523/JNEUROSCI.17-05-01596.1997. PMC 6573372. PMID 9030619.
  14. ^ a b 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. doi:10.1016/s0896-6273(02)00583-4. PMID 11832227. S2CID 17878965.
  15. ^ a b 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. doi:10.4049/jimmunol.164.11.5850. PMID 10820264.
  16. ^ 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. doi:10.1016/s0003-9969(03)00116-x. PMID 12828989.
  17. ^ 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. doi:10.1074/jbc.275.11.8240. PMID 10713150.
  18. ^ 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. doi:10.1093/emboj/18.16.4372. PMC 1171512. PMID 10449403.
  19. ^ McMahon HT, Missler M, Li C, Südhof TC (Oct 1995). "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell. 83 (1): 111–9. doi:10.1016/0092-8674(95)90239-2. PMID 7553862. S2CID 675343.
  20. ^ 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. doi:10.1006/mcne.2002.1122. PMID 12093152. S2CID 23927545.
  21. ^ 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. doi:10.1016/s0014-5793(99)00028-9. PMID 10100611. S2CID 9115709.
  22. ^ 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. doi:10.4049/jimmunol.170.2.1034. PMID 12517971.
  23. ^ 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. doi:10.1042/bj3170945. PMC 1217577. PMID 8760387.
  24. ^ 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. doi:10.1182/blood.V93.8.2617. PMID 10194441.

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