SYT1

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Synaptotagmin I
Protein SYT1 PDB 1byn.png
PDB rendering based on 1byn.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols SYT1 ; P65; SVP65; SYT
External IDs OMIM185605 MGI99667 HomoloGene4122 ChEMBL: 1953 GeneCards: SYT1 Gene
RNA expression pattern
PBB GE SYT1 203999 at tn.png
PBB GE SYT1 203998 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6857 20979
Ensembl ENSG00000067715 ENSMUSG00000035864
UniProt P21579 P46096
RefSeq (mRNA) NM_001135805 NM_001252341
RefSeq (protein) NP_001129277 NP_001239270
Location (UCSC) Chr 12:
79.26 – 79.85 Mb
Chr 10:
108.5 – 109.01 Mb
PubMed search [1] [2]

Synaptotagmin-1 is a protein that in humans is encoded by the SYT1 gene.[1]

The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin I participates in triggering neurotransmitter release at the synapse (Fernandez-Chacon et al., 2001).[supplied by OMIM][2]

SYT1 is the master switch responsible for allowing the human brain to release neurotransmitters. SYT1 senses calcium concentrations as low as 10 ppm and subsequently signals the SNARE complex to open fusion pores.[3]

Interactions[edit]

SYT1 has been shown to interact with SNAP-25,[4][5] STX1A[6][7] and S100A13.[8][9]

References[edit]

  1. ^ Perin MS, Johnston PA, Ozcelik T, Jahn R, Francke U, Sudhof TC (February 1991). "Structural and functional conservation of synaptotagmin (p65) in Drosophila and humans". J Biol Chem 266 (1): 615–22. PMID 1840599. 
  2. ^ "Entrez Gene: SYT1 synaptotagmin I". 
  3. ^ Lee HK, Yang Y, Su Z, Hyeon C, Lee TS, Lee HW, Kweon DH, Shin YK, Yoon TY (May 2010). "Dynamic Ca2+-Dependent Stimulation of Vesicle Fusion by Membrane-Anchored Synaptotagmin 1". Science 328 (5979): 760–3. doi:10.1126/science.1187722. PMC 2994549. PMID 20448186. Lay summarysciencedaily.com. 
  4. ^ Gerona, R R; Larsen E C, Kowalchyk J A, Martin T F (March 2000). "The C terminus of SNAP25 is essential for Ca(2+)-dependent binding of synaptotagmin to SNARE complexes". J. Biol. Chem. (UNITED STATES) 275 (9): 6328–36. doi:10.1074/jbc.275.9.6328. ISSN 0021-9258. PMID 10692432. 
  5. ^ Zhang, Xiaodong; Kim-Miller Mindy J, Fukuda Mitsunori, Kowalchyk Judith A, Martin Thomas F J (May 2002). "Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis". Neuron (United States) 34 (4): 599–611. doi:10.1016/S0896-6273(02)00671-2. ISSN 0896-6273. PMID 12062043. 
  6. ^ Shao, X; Li C, Fernandez I, Zhang X, Südhof T C, Rizo J (January 1997). "Synaptotagmin-syntaxin interaction: the C2 domain as a Ca2+-dependent electrostatic switch". Neuron (UNITED STATES) 18 (1): 133–42. doi:10.1016/S0896-6273(01)80052-0. ISSN 0896-6273. PMID 9010211. 
  7. ^ Thomas, D M; Ferguson G D, Herschman H R, Elferink L A (July 1999). "Functional and Biochemical Analysis of the C2 Domains of Synaptotagmin IV". Mol. Biol. Cell (UNITED STATES) 10 (7): 2285–95. doi:10.1091/mbc.10.7.2285. ISSN 1059-1524. PMC 25443. PMID 10397765. 
  8. ^ Mouta Carreira, C; LaVallee T M, Tarantini F, Jackson A, Lathrop J T, Hampton B, Burgess W H, Maciag T (August 1998). "S100A13 is involved in the regulation of fibroblast growth factor-1 and p40 synaptotagmin-1 release in vitro". J. Biol. Chem. (UNITED STATES) 273 (35): 22224–31. doi:10.1074/jbc.273.35.22224. ISSN 0021-9258. PMID 9712836. 
  9. ^ Landriscina, M; Bagalá C, Mandinova A, Soldi R, Micucci I, Bellum S, Prudovsky I, Maciag T (July 2001). "Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress". J. Biol. Chem. (United States) 276 (27): 25549–57. doi:10.1074/jbc.M102925200. ISSN 0021-9258. PMID 11432880. 

Further reading[edit]