Synaptotagmin-1 is a
protein that in humans is encoded by the SYT1gene.[5]
Function
Synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as sensors for calcium ions (Ca2+) in the process of vesicular trafficking and exocytosis. Calcium ion binding to synaptotagmin I participates in triggering neurotransmitter release at the synapse.[6] [Supplied by
OMIM[7]
SYT1 is the master switch responsible for allowing the human brain to release neurotransmitters. SYT1 senses calcium ion concentrations as low as 10 ppm and subsequently signals the
SNARE complex to open fusion pores.[8]
Mochly-Rosen D, Miller KG, Scheller RH, Khaner H, Lopez J, Smith BL (Sep 1992). "p65 fragments, homologous to the C2 region of protein kinase C, bind to the intracellular receptors for protein kinase C". Biochemistry. 31 (35): 8120–4.
doi:
10.1021/bi00150a003.
PMID1326322.
O'Regan S, Diebler MF, Meunier FM, Vyas S (Jan 1995). "A Ewing's sarcoma cell line showing some, but not all, of the traits of a cholinergic neuron". Journal of Neurochemistry. 64 (1): 69–76.
doi:
10.1046/j.1471-4159.1995.64010069.x.
PMID7798952.
S2CID20958851.
Zhang JZ, Davletov BA, Südhof TC, Anderson RG (Sep 1994). "Synaptotagmin I is a high affinity receptor for clathrin AP-2: implications for membrane recycling". Cell. 78 (5): 751–60.
doi:
10.1016/S0092-8674(94)90442-1.
PMID8087843.
S2CID44550431.
Perin MS (Oct 1996). "Mirror image motifs mediate the interaction of the COOH terminus of multiple synaptotagmins with the neurexins and calmodulin". Biochemistry. 35 (43): 13808–16.
doi:
10.1021/bi960853x.
PMID8901523.
Fernández-Chacón R, Königstorfer A, Gerber SH, García J, Matos MF, Stevens CF, Brose N, Rizo J, Rosenmund C, Südhof TC (Mar 2001). "Synaptotagmin I functions as a calcium regulator of release probability". Nature. 410 (6824): 41–9.
doi:
10.1038/35065004.
PMID11242035.
S2CID1756258.
Fukuda M, Mikoshiba K (Mar 2001). "Synaptotagmin-like protein 1-3: a novel family of C-terminal-type tandem C2 proteins". Biochemical and Biophysical Research Communications. 281 (5): 1226–33.
doi:
10.1006/bbrc.2001.4512.
PMID11243866.
Synaptotagmin-1 is a
protein that in humans is encoded by the SYT1gene.[5]
Function
Synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as sensors for calcium ions (Ca2+) in the process of vesicular trafficking and exocytosis. Calcium ion binding to synaptotagmin I participates in triggering neurotransmitter release at the synapse.[6] [Supplied by
OMIM[7]
SYT1 is the master switch responsible for allowing the human brain to release neurotransmitters. SYT1 senses calcium ion concentrations as low as 10 ppm and subsequently signals the
SNARE complex to open fusion pores.[8]
Mochly-Rosen D, Miller KG, Scheller RH, Khaner H, Lopez J, Smith BL (Sep 1992). "p65 fragments, homologous to the C2 region of protein kinase C, bind to the intracellular receptors for protein kinase C". Biochemistry. 31 (35): 8120–4.
doi:
10.1021/bi00150a003.
PMID1326322.
O'Regan S, Diebler MF, Meunier FM, Vyas S (Jan 1995). "A Ewing's sarcoma cell line showing some, but not all, of the traits of a cholinergic neuron". Journal of Neurochemistry. 64 (1): 69–76.
doi:
10.1046/j.1471-4159.1995.64010069.x.
PMID7798952.
S2CID20958851.
Zhang JZ, Davletov BA, Südhof TC, Anderson RG (Sep 1994). "Synaptotagmin I is a high affinity receptor for clathrin AP-2: implications for membrane recycling". Cell. 78 (5): 751–60.
doi:
10.1016/S0092-8674(94)90442-1.
PMID8087843.
S2CID44550431.
Perin MS (Oct 1996). "Mirror image motifs mediate the interaction of the COOH terminus of multiple synaptotagmins with the neurexins and calmodulin". Biochemistry. 35 (43): 13808–16.
doi:
10.1021/bi960853x.
PMID8901523.
Fernández-Chacón R, Königstorfer A, Gerber SH, García J, Matos MF, Stevens CF, Brose N, Rizo J, Rosenmund C, Südhof TC (Mar 2001). "Synaptotagmin I functions as a calcium regulator of release probability". Nature. 410 (6824): 41–9.
doi:
10.1038/35065004.
PMID11242035.
S2CID1756258.
Fukuda M, Mikoshiba K (Mar 2001). "Synaptotagmin-like protein 1-3: a novel family of C-terminal-type tandem C2 proteins". Biochemical and Biophysical Research Communications. 281 (5): 1226–33.
doi:
10.1006/bbrc.2001.4512.
PMID11243866.