Phosphorylation of SLP-76 by p-SYK

Stable Identifier
Reaction [transition]
Homo sapiens
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SLP-76 lacks intrinsic catalytic activity and acts as a scaffold, recruiting other proteins for correct localization during molecular signal transduction (Bogin et al. 2007). Activation of FCERI leads to tyrosine phosphorylation of SLP-76 (Gross et al. 1999). SLP-76 has three potential tyrosine phosphorylation sites within its amino terminus region: Y113, Y128, and Y145. Phosphorylation may be mediated by SYK, analogous to the role of ZAP-70 in phosphorylating T-cell SLP-76 (Bubeck-Wardenberg et al. 1996).

Literature References
PubMed ID Title Journal Year
10026222 Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets

Gross, BS, Lee, JR, Clements, JL, Turner, M, Tybulewicz, VL, Findell, PR, Koretzky, GA, Watson, SP

J Biol Chem 1999
19592646 SLP-76 couples Syk to the osteoclast cytoskeleton

Reeve, JL, Zou, W, Liu, Y, Maltzman, JS, Ross, FP, Teitelbaum, SL

J Immunol 2009
8995445 SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells

Hendricks-Taylor, LR, Motto, DG, Zhang, J, Siraganian, RP, Koretzky, GA

J. Biol. Chem. 1997
8702662 Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function

Bubeck Wardenburg, J, Fu, C, Jackman, JK, Flotow, H, Wilkinson, SE, Williams, DH, Johnson, R, Kong, G, Chan, AC, Findell, PR

J Biol Chem 1996
Participant Of
Catalyst Activity
Catalyst Activity
protein tyrosine kinase activity of Clustered p:LYN:p-FCERI:IgE:allergin:p-6Y-SYK [plasma membrane]
Physical Entity
Orthologous Events
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