SYK autophosphorylates

Stable Identifier
R-HSA-453200
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
11481033 Structure and function of Syk protein-tyrosine kinase

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

J Biochem 2001
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
19409513 Conformational rearrangements upon Syk auto-phosphorylation

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

Biochim Biophys Acta 2009
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
non-membrane spanning protein tyrosine kinase activity of GPVI:phosphorylated Fc Epsilon R1 gamma:FYN:LYN:Collagen type I:SYK [plasma membrane]
Physical Entity
Activity
This event is regulated
Orthologous Events
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Created