Syk

aus Wikipedia, der freien Enzyklopädie
Wechseln zu: Navigation, Suche
Tyrosine-protein kinase SYK
Tyrosine-protein kinase SYK
nach PDB 1A81
Andere Namen

Spleen tyrosine kinase, p72-Syk

Vorhandene Strukturdaten: PDB 1CSY, PDB 1CSZ
Eigenschaften des menschlichen Proteins
Masse/Länge Primärstruktur 635 Aminosäuren, 72.066 Da
Bezeichner
Externe IDs
Enzymklassifikation
EC, Kategorie 2.7.10.2
Orthologe (Mensch)
Entrez 6850
Ensembl ENSG00000165025
UniProt P43405
Refseq (mRNA) NM_001135052.3
Refseq (Protein) NP_001128524.1
PubMed-Suche 6850

SYK ist ein Enzym aus der Gruppe der Tyrosinkinasen.

Eigenschaften[Bearbeiten | Quelltext bearbeiten]

Als Tyrosinkinase phosphoryliert Syk Tyrosine in Proteinen. Syk besitzt eine SH2-Proteindomäne und bindet damit an aktivierte Rezeptor-Tyrosinkinasen in der Zellmembran. In Folge einer Aktivierung von Syk werden VAV1, PLCG1, PI-3-Kinase, LCP2 und BLNK phosphoryliert. Syk ist phosphoryliert.

Syk katalysiert die Reaktion: ATP + [Protein]-L-Tyrosin = ADP + [Protein]-L-Tyrosinphosphat

Syk bindet an Cbl,[1][2][3] CRKL,[4] FCGR2A,[5][6] FYN,[7][8] Grb2,[9][10] Lck,[11] LYN,[12] PTK2,[13] PTPN6,[9][14] und VAV1.[1][15][16]

Weblinks[Bearbeiten | Quelltext bearbeiten]

Einzelnachweise[Bearbeiten | Quelltext bearbeiten]

  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, Nr. 4, April 2001, S. 193–200. PMID 11331248.
  2. Lupher ML, Rao N, Lill NL, Andoniou CE, Miyake S, Clark EA, Druker B, Band 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, Nr. 52, December 1998, S. 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, Nr. Pt 2, March 2003, S. 687–94. doi:10.1042/BJ20021201. PMID 12435267. PMC 1223185 (freier Volltext).
  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, Nr. 9, May 2001, S. 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, Nr. 3, July 1997, S. 348–58. doi:10.1016/S0167-4889(97)00034-7. PMID 9268059.
  6. Kim MK, Pan XQ, Huang ZY, Hunter S, Hwang PH, Indik 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, Nr. 1, January 2001, S. 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, Nr. 15, April 1998, S. 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, Nr. 23, June 1997, S. 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, Nr. 23, June 2000, S. 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, Nr. Pt 3, May 2002, S. 717–25. doi:10.1042/0264-6021:3630717. PMID 11964172. PMC 1222524 (freier Volltext).
  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, Nr. 6, June 1995, S. 1997–2006. doi:10.1084/jem.181.6.1997. PMID 7539035. PMC 2192070 (freier Volltext).
  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 of the United States of America. 92, Nr. 2, January 1995, S. 359–63. doi:10.1073/pnas.92.2.359. PMID 7831290. PMC 42739 (freier Volltext).
  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, Nr. 3, September 1997, S. 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, Nr. 5, March 1999, S. 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, Nr. 6, December 1996, S. 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, Nr. 43, October 1996, S. 26962–70. doi:10.1074/jbc.271.43.26962. PMID 8900182.