Reactome | SYK autophosphorylates

SYK autophosphorylates

Stable Identifier

R-HSA-453200

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol, plasma membrane

ReviewStatus

5/5

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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 Taniguchi, T, Kobayashi, T, Kondo, J, Takahashi, K, Nakamura, H, Suzuki, J, Nagai, K, Yamada, T, Nakamura, S, Yamamura, H	J Biol Chem	1991
11481033	Structure and function of Syk protein-tyrosine kinase Sada, K, Takano, T, Yanagi, S, Yamamura, H	J Biochem	2001
19409513	Conformational rearrangements upon Syk auto-phosphorylation Arias-Palomo, E, Recuero-Checa, MA, Bustelo, XR, Llorca, O	Biochim Biophys Acta	2009