SYK autophosphorylates

Stable Identifier
Reaction [transition]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Binding of Syk causes conformational changes that lead to Syk activation by autophosphorylation. Syk can be activated by a number of phosphorylation events, and it has been proposed that Syk may function as a switch whereby any of several possible stimuli trigger the acquisition of similar activated conformations. (Tsang et al. 2008). These phosphorylations both modulate Syk's catalytic activity (Keshvara et al. 1997) and generate docking sites for SH2 domain-containing proteins, such as c-Cbl, PLC, and Vav1. Syk tyrosine phosphorylation is reduced in the presence of the ITIM-containing immunoglobulin superfamily transmembrane protein G6B (Mori et al. 2008).

Literature References
PubMed ID Title Journal Year
1874735 Molecular cloning of a porcine gene syk that encodes a 72-kDa protein-tyrosine kinase showing high susceptibility to proteolysis

Nagai, K, Suzuki, J, Kobayashi, T, Taniguchi, T, Yamada, T, Nakamura, H, Kondo, J, Yamamura, H, Takahashi, K, Nakamura, S

J Biol Chem 1991
11481033 Structure and function of Syk protein-tyrosine kinase

Yamamura, H, Sada, K, Yanagi, S, Takano, T

J Biochem 2001
19409513 Conformational rearrangements upon Syk auto-phosphorylation

Recuero-Checa, MA, Llorca, O, Bustelo, XR, Arias-Palomo, E

Biochim Biophys Acta 2009
Catalyst Activity

non-membrane spanning protein tyrosine kinase activity of GPVI:phosphorylated Fc Epsilon R1 gamma:FYN:LYN:Collagen type I:SYK [plasma membrane]

This event is regulated
Orthologous Events
Cite Us!