SYT1

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SYT1
Protein SYT1 PDB 1byn.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases SYT1, P65, SVP65, SYT, synaptotagmin 1
External IDs MGI: 99667 HomoloGene: 4122 GeneCards: SYT1
Genetically Related Diseases
obesity[1]
RNA expression pattern
PBB GE SYT1 203998 s at fs.png

PBB GE SYT1 203999 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001135805
NM_001135806
NM_001291901
NM_005639

NM_001252341
NM_001252342
NM_009306

RefSeq (protein)

NP_001129277
NP_001129278
NP_001278830
NP_005630

Location (UCSC) Chr 12: 78.86 – 79.45 Mb Chr 10: 108.5 – 109.01 Mb
PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Synaptotagmin-1 is a protein that in humans is encoded by the SYT1 gene.[4]

Function[edit]

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][5]

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.[6]

Interactions[edit]

SYT1 has been shown to interact with SNAP-25,[7][8] STX1A[9][10] and S100A13.[11][12]

References[edit]

  1. ^ "Diseases that are genetically associated with SYT1 view/edit references on wikidata". 
  2. ^ "Human PubMed Reference:". 
  3. ^ "Mouse PubMed Reference:". 
  4. ^ Perin MS, Johnston PA, Ozcelik T, Jahn R, Francke U, Südhof TC (Jan 1991). "Structural and functional conservation of synaptotagmin (p65) in Drosophila and humans". The Journal of Biological Chemistry. 266 (1): 615–22. PMID 1840599. 
  5. ^ "Entrez Gene: SYT1 synaptotagmin I". 
  6. ^ 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 2994549Freely accessible. PMID 20448186. Lay summarysciencedaily.com. 
  7. ^ Gerona RR, Larsen EC, Kowalchyk JA, Martin TF (Mar 2000). "The C terminus of SNAP25 is essential for Ca(2+)-dependent binding of synaptotagmin to SNARE complexes". The Journal of Biological Chemistry. 275 (9): 6328–36. doi:10.1074/jbc.275.9.6328. PMID 10692432. 
  8. ^ Zhang X, Kim-Miller MJ, Fukuda M, Kowalchyk JA, Martin TF (May 2002). "Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis". Neuron. 34 (4): 599–611. doi:10.1016/S0896-6273(02)00671-2. PMID 12062043. 
  9. ^ Shao X, Li C, Fernandez I, Zhang X, Südhof TC, Rizo J (Jan 1997). "Synaptotagmin-syntaxin interaction: the C2 domain as a Ca2+-dependent electrostatic switch". Neuron. 18 (1): 133–42. doi:10.1016/S0896-6273(01)80052-0. PMID 9010211. 
  10. ^ Thomas DM, Ferguson GD, Herschman HR, Elferink LA (Jul 1999). "Functional and biochemical analysis of the C2 domains of synaptotagmin IV". Molecular Biology of the Cell. 10 (7): 2285–95. doi:10.1091/mbc.10.7.2285. PMC 25443Freely accessible. PMID 10397765. 
  11. ^ Mouta Carreira C, LaVallee TM, Tarantini F, Jackson A, Lathrop JT, Hampton B, Burgess WH, Maciag T (Aug 1998). "S100A13 is involved in the regulation of fibroblast growth factor-1 and p40 synaptotagmin-1 release in vitro". The Journal of Biological Chemistry. 273 (35): 22224–31. doi:10.1074/jbc.273.35.22224. PMID 9712836. 
  12. ^ Landriscina M, Bagalá C, Mandinova A, Soldi R, Micucci I, Bellum S, Prudovsky I, Maciag T (Jul 2001). "Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress". The Journal of Biological Chemistry. 276 (27): 25549–57. doi:10.1074/jbc.M102925200. PMID 11432880. 

Further reading[edit]