Syk

from Wikipedia, the free encyclopedia
Tyrosine protein kinase SYK
Tyrosine protein kinase SYK
according to PDB  1A81
other names

Spleen tyrosine kinase, p72-Syk

Existing structure data : PDB  1CSY , PDB  1CSZ

Properties of human protein
Mass / length primary structure 635 amino acids , 72,066 Da
Identifier
External IDs
Enzyme classification
EC, category 2.7.10.2
Orthologue (human)
Entrez 6850
Ensemble ENSG00000165025
UniProt P43405
Refseq (mRNA) NM_001135052.3
Refseq (protein) NP_001128524.1
PubMed search 6850

SYK is an enzyme from the group of tyrosine kinases .

properties

As a tyrosine kinase, Syk phosphorylates tyrosine in proteins . Syk has an SH2 protein domain and thus binds to activated receptor tyrosine kinases in the cell membrane . As a result of activation of Syk, VAV1 , PLCG1 , PI-3-kinase , LCP2 and BLNK are phosphorylated. Syk is phosphorylated.

Syk catalyzes the reaction: ATP + [protein] -L-tyrosine = ADP + [protein] -L-tyrosine phosphate

Syk binds to Cbl , CRKL , FCGR2A , FYN , Grb2 , Lck , LYN , PTK2 , PTPN6 , and VAV1 .

Web links

Individual evidence

  1. ^ A b Bertagnolo V, Marchisio M, Brugnoli F, Bavelloni A, Boccafogli L, Colamussi ML, Capitani S: Requirement of tyrosine-phosphorylated Vav for morphological differentiation of all-trans-retinoic acid-treated HL-60 cells . In: Cell Growth & Differentiation . 12, No. 4, April 2001, pp. 193-200. PMID 11331248 .
  2. ↑ Lupher ML, Rao N, Lill NL, Andoniou CE, Miyake S, Clark EA, Druker B, Volume H: Cbl-mediated negative regulation of the Syk tyrosine kinase. A critical role for Cbl phosphotyrosine-binding domain binding to Syk phosphotyrosine 323 . In: The Journal of Biological Chemistry . 273, No. 52, December 1998, pp. 35273-81. doi : 10.1074 / jbc.273.52.35273 . PMID 9857068 .
  3. ↑ Melander F, Andersson T, Dib K: Fgr but not Syk tyrosine kinase is a target for beta 2 integrin-induced c-Cbl-mediated ubiquitination in adherent human neutrophils . In: The Biochemical Journal . 370, No. Pt 2, March 2003, pp. 687-94. doi : 10.1042 / BJ20021201 . PMID 12435267 . PMC 1223185 (free full text).
  4. ↑ Oda A, Ochs HD, Lasky LA, Spencer S, Ozaki K, Fujihara M, Handa M, Ikebuchi K, Ikeda H: CrkL is an adapter for Wiskott-Aldrich syndrome protein and Syk . In: Blood . 97, No. 9, May 2001, pp. 2633-9. doi : 10.1182 / blood.V97.9.2633 . PMID 11313252 .
  5. ↑ Ibarrola I, Vossebeld PJ, Homburg CH, Thelen M, Roos D, Verhoeven AJ: Influence of tyrosine phosphorylation on protein interaction with FcgammaRIIa . In: Biochimica et Biophysica Acta . 1357, No. 3, July 1997, pp. 348-58. doi : 10.1016 / S0167-4889 (97) 00034-7 . PMID 9268059 .
  6. ↑ Kim MK, Pan XQ, Huang ZY, Hunter S, Hwang PH, Indic ZK, Schreiber AD: Fc gamma receptors differ in their structural requirements for interaction with the tyrosine kinase Syk in the initial steps of signaling for phagocytosis . In: Clinical Immunology . 98, No. 1, January 2001, pp. 125-32. doi : 10.1006 / clim.2000.4955 . PMID 11141335 .
  7. ↑ Deckert M, Elly C, Altman A, Liu YC: Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases . In: The Journal of Biological Chemistry . 273, No. 15, April 1998, pp. 8867-74. doi : 10.1074 / jbc.273.15.8867 . PMID 9535867 .
  8. ↑ Chung J, Gao AG, Frazier WA: Thrombspondin acts via integrin-associated protein to activate the platelet integrin alphaIIbbeta3 . In: The Journal of Biological Chemistry . 272, No. 23, June 1997, pp. 14740-6. doi : 10.1074 / jbc.272.23.14740 . PMID 9169439 .
  9. ↑ a b Ganju RK, Brubaker SA, Chernock RD, Avraham S, Groopman JE: Beta-chemokine receptor CCR5 signals through SHP1, SHP2, and Syk . In: The Journal of Biological Chemistry . 275, No. 23, June 2000, pp. 17263-8. doi : 10.1074 / jbc.M000689200 . PMID 10747947 .
  10. ↑ Saci A, Liu WQ, Vidal M, Garbay C, Rendu F, Bachelot-Loza C: Differential effect of the inhibition of Grb2-SH3 interactions in platelet activation induced by thrombin and by Fc receptor engagement . In: The Biochemical Journal . 363, No. Pt 3, May 2002, pp. 717-25. doi : 10.1042 / 0264-6021: 3630717 . PMID 11964172 . PMC 1222524 (free full text).
  11. ↑ Thome M, Duplay P, Guttinger M, Acuto O: Syk and ZAP-70 mediate recruitment of p56lck / CD4 to the activated T cell receptor / CD3 / zeta complex . In: The Journal of Experimental Medicine . 181, No. 6, June 1995, pp. 1997-2006. doi : 10.1084 / jem.181.6.1997 . PMID 7539035 . PMC 2192070 (free full text).
  12. ↑ Sidorenko SP, Law CL, Chandran KA, Clark EA: Human spleen tyrosine kinase p72Syk associates with the Src-family kinase p53 / 56Lyn and a 120-kDa phosphoprotein . In: Proceedings of the National Academy of Sciences . 92, No. 2, January 1995, pp. 359-63. doi : 10.1073 / pnas.92.2.359 . PMID 7831290 . PMC 42739 (free full text).
  13. ↑ Sada K, Minami Y, Yamamura H: Relocation of Syk protein-tyrosine kinase to the actin filament network and subsequent association with Fak . In: European Journal of Biochemistry . 248, No. 3, September 1997, pp. 827-33. doi : 10.1111 / j.1432-1033.1997.00827.x . PMID 9342235 .
  14. ↑ Dustin LB, Plas DR, Wong J, Hu YT, Soto C, Chan AC, Thomas ML: Expression of dominant-negative src-homology domain 2-containing protein tyrosine phosphatase-1 results in increased Syk tyrosine kinase activity and B cell activation . In: Journal of Immunology . 162, No. 5, March 1999, pp. 2717-24. PMID 10072516 .
  15. ↑ Deckert M, Tartare-Deckert S, Couture C, Mustelin T, Altman A: Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product . In: Immunity . 5, No. 6, December 1996, pp. 591-604. doi : 10.1016 / S1074-7613 (00) 80273-3 . PMID 8986718 .
  16. ^ Song JS, Gomez J, Stancato LF, Rivera J: Association of a p95 Vav-containing signaling complex with the FcepsilonRI gamma chain in the RBL-2H3 mast cell line. Evidence for a constitutive in vivo association of Vav with Grb2, Raf-1, and ERK2 in an active complex . In: The Journal of Biological Chemistry . 271, No. 43, October 1996, pp. 26962-70. doi : 10.1074 / jbc.271.43.26962 . PMID 8900182 .