Phosphorylation of SLP-76 by p-SYK

Stable Identifier
R-HSA-2396594
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

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 DAP12-associated receptors 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
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
Participants
Participant Of
hasEvent
Catalyst Activity
Catalyst Activity
Title
protein tyrosine kinase activity of DAP12 Receptors:p-DAP12:p-6Y-SYK [plasma membrane]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed