Phosphorylation of syk

Stable Identifier
R-RNO-2054095
Type
Reaction [transition]
Species
Rattus norvegicus
Compartment
General
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Phosphorylation of syk

Multiple sites of phosphorylation are known to exist in SYK, which both regulate its activity and also serve as docking sites for other proteins. Some of these sites include Y131 of interdomain A, Y323, Y348, and Y352 of interdomain B, and 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). Phosphorylation of these tyrosine residues disrupts autoinhibitory interactions and results in kinase activation even in the absence of phosphorylated ITAM tyrosines (Tsang et al. 2008). SYK is primarily phosphorylated by Src family kinases and this acts as an initiating trigger by generating few molecules of activated SYK which are then involved in major SYK autophosphorylation (Hillal et al. 1997).

Literature References
PubMed ID Title Journal Year
10931839 Phosphorylation of Syk activation loop tyrosines is essential for Syk function. An in vivo study using a specific anti-Syk activation loop phosphotyrosine antibody

Zhang, J, Billingsley, ML, Kincaid, RL, Siraganian, RP

J Biol Chem 2000
Participants
Catalyst Activity
Catalyst Activity
Title
protein tyrosine kinase activity of Syk [cytosol]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created