SYT2
From Wikipedia the free encyclopedia
Synaptotagmin-2 is a protein that in humans is encoded by the SYT2 gene.[5][6]
References[edit]
- ^ a b c GRCh38: Ensembl release 89: ENSG00000143858 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026452 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Jones JM, Popma SJ, Mizuta M, Seino S, Meisler MH (March 1995). "Synaptotagmin genes on mouse chromosomes 1, 7, and 10 and human chromosome 19". Mammalian Genome. 6 (3): 212–3. doi:10.1007/BF00293017. hdl:2027.42/47020. PMID 7749232. S2CID 24653745.
- ^ "Entrez Gene: SYT2 synaptotagmin II".
Further reading[edit]
- Fukuda M, Aruga J, Niinobe M, Aimoto S, Mikoshiba K (November 1994). "Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II". The Journal of Biological Chemistry. 269 (46): 29206–11. doi:10.1016/S0021-9258(19)62031-4. PMID 7961887.
- Perin MS (October 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. PMID 8901523.
- Baram D, Adachi R, Medalia O, Tuvim M, Dickey BF, Mekori YA, Sagi-Eisenberg R (May 1999). "Synaptotagmin II negatively regulates Ca2+-triggered exocytosis of lysosomes in mast cells". The Journal of Experimental Medicine. 189 (10): 1649–58. doi:10.1084/jem.189.10.1649. PMC 2193646. PMID 10330444.
- Mizutani A, Fukuda M, Ibata K, Shiraishi Y, Mikoshiba K (March 2000). "SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear ribonucleoprotein R, interacts with ubiquitous synaptotagmin isoforms". The Journal of Biological Chemistry. 275 (13): 9823–31. doi:10.1074/jbc.275.13.9823. PMID 10734137.
- Kida Y, Sakaguchi M, Fukuda M, Mikoshiba K, Mihara K (August 2000). "Membrane topogenesis of a type I signal-anchor protein, mouse synaptotagmin II, on the endoplasmic reticulum". The Journal of Cell Biology. 150 (4): 719–30. doi:10.1083/jcb.150.4.719. PMC 2175286. PMID 10952998.
- Martina JA, Bonangelino CJ, Aguilar RC, Bonifacino JS (May 2001). "Stonin 2: an adaptor-like protein that interacts with components of the endocytic machinery". The Journal of Cell Biology. 153 (5): 1111–20. doi:10.1083/jcb.153.5.1111. PMC 2174325. PMID 11381094.
- Kida Y, Sakaguchi M, Fukuda M, Mikoshiba K, Mihara K (November 2001). "Amino acid residues before the hydrophobic region which are critical for membrane translocation of the N-terminal domain of synaptotagmin II". FEBS Letters. 507 (3): 341–5. doi:10.1016/S0014-5793(01)03000-9. PMID 11696368. S2CID 29026112.
- Lindmark IM, Karlsson A, Serrander L, Francois P, Lew D, Rasmusson B, Stendahl O, Nüsse O (June 2002). "Synaptotagmin II could confer Ca(2+) sensitivity to phagocytosis in human neutrophils". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1590 (1–3): 159–66. doi:10.1016/S0167-4889(02)00209-4. PMID 12063179.
- Rickman C, Archer DA, Meunier FA, Craxton M, Fukuda M, Burgoyne RD, Davletov B (March 2004). "Synaptotagmin interaction with the syntaxin/SNAP-25 dimer is mediated by an evolutionarily conserved motif and is sensitive to inositol hexakisphosphate". The Journal of Biological Chemistry. 279 (13): 12574–9. doi:10.1074/jbc.M310710200. PMID 14709554.
- Lee BH, Min X, Heise CJ, Xu BE, Chen S, Shu H, Luby-Phelps K, Goldsmith EJ, Cobb MH (September 2004). "WNK1 phosphorylates synaptotagmin 2 and modulates its membrane binding". Molecular Cell. 15 (5): 741–51. doi:10.1016/j.molcel.2004.07.018. PMID 15350218.
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