[HTML][HTML] Molecular basis for a direct interaction between the Syk protein-tyrosine kinase and phosphoinositide 3-kinase

KD Moon, CB Post, DL Durden, Q Zhou, P De… - Journal of Biological …, 2005 - ASBMB
After engagement of the B cell receptor for antigen, the Syk protein-tyrosine kinase becomes
phosphorylated on multiple tyrosines, some of which serve as docking sites for downstream
effectors with SH2 or other phosphotyrosine binding domains. The most frequently identified
binding partner for catalytically active Syk identified in a yeast two-hybrid screen was the
p85 regulatory subunit of phosphoinositide 3-kinase. The C-terminal SH2 domain of p85
was sufficient for mediating an interaction with tyrosine-phosphorylated Syk. Interestingly …