Reactome | Phosphorylation of SLP-76 by p-SYK

Phosphorylation of SLP-76 by p-SYK

Stable Identifier

R-HSA-2396594

Type

Reaction [transition]

Species

Homo sapiens

Compartment

plasma membrane

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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 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