Tyrosine-phosphorylated SOCS3 Interacts with the Nck and Crk-L Adapter Proteins and Regulates Nck Activation

摘要: Suppressors of cytokine signaling (SOCS) are negative feedback inhibitors and growth factor signal transduction. Although the affect SOCS proteins on Jak-STAT pathway has been well characterized, their role in regulation other modules is not understood. In present study, we demonstrate that SOCS3 physically interacts with SH2/SH3-containing adapter Nck Crk-L, which known to couple activated receptors multiple downstream pathways actin cytoskeleton. Our data show SOCS3/Nck SOCS3/Crk-L interactions depend tyrosine phosphorylation Tyr221 within conserved box motif intact SH2 domains Crk-L. Furthermore, forms a YXXP motif, consensus binding site for Crk-L domains. Expression NIH3T3 cells induces constitutive recruitment Nck-GFP fusion protein plasma membrane endogenous Nck. findings suggest regulates factor-activated by acting as proteins.