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

ReviewStatus

5/5

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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
19592646	SLP-76 couples Syk to the osteoclast cytoskeleton Teitelbaum, SL, Ross, FP, Maltzman, JS, Liu, Y, Reeve, JL, Zou, W	J Immunol	2009
10026222	Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets Watson, SP, Turner, M, Tybulewicz, VL, Lee, JR, Gross, BS, Clements, JL, Koretzky, GA, Findell, PR	J Biol Chem	1999
8702662	Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function Bubeck Wardenburg, J, Johnson, R, Williams, DH, Jackman, JK, Flotow, H, Chan, AC, Wilkinson, SE, Fu, C, Findell, PR, Kong, G	J Biol Chem	1996