Phosphorylation of SYK

Stable Identifier
Reaction [transition]
Homo sapiens
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The binding of SYK to DAP12 induces conformational changes that result in SYK activation. Around ten autophosporylated tyrosine residues have been identified in SYK, regulating activity and serving as docking sites for other proteins. Sites include Y131 of interdomain A, Y323, Y348, and Y352 of interdomain B, Y525 and Y526 within the activation loop of the kinase domain and Y630 in the C-terminus (Zhang et al. 2002, Lupher et al. 1998, Furlong et al. 1997).

SYK is phosphorylated by Src family kinases and this acts as an initiating trigger by generating a few molecules of activated SYK, which then initiate SYK autophosphorylation (Hillal et al. 1997, Castro et al. 2010)
Literature References
PubMed ID Title Journal Year
9396765 Functional role for Syk tyrosine kinase in natural killer cell-mediated natural cytotoxicity

Ten, RM, Dick, CJ, Leibson, PJ, Billadeau, DD, Binstadt, BA, Brumbaugh, KM, Schoon, RA

J. Exp. Med. 1997
9830044 DAP12-mediated signal transduction in natural killer cells. A dominant role for the Syk protein-tyrosine kinase

Ortaldo, JR, Nakamura, MC, Gosselin, P, McVicar, DW, Taylor, LS, Linnemeyer, P, Mikhael, AI, Seaman, WE, Geahlen, RL, Mason, LH, Anderson, SK, Willette-Brown, J

J. Biol. Chem. 1998
Catalyst Activity

protein tyrosine kinase activity of DAP12 receptors:p-DAP12:SYK [plasma membrane]

Orthologous Events
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