Inhibition of SHP2-mediated dephosphorylation of Ras suppresses oncogenesis

Abstract excerpt

Ras is phosphorylated on a conserved tyrosine at position 32 within the switch I region via Src kinase. This phosphorylation inhibits the binding of effector Raf while promoting the engagement of GTPase-activating protein (GAP) and GTP hydrolysis. Here we identify SHP2 as the ubiquitously expressed tyrosine phosphatase that preferentially binds to and dephosphorylates Ras to increase its association with Raf and...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Cytokine Signaling Pathways and Interactions
• Share to Melanoma and MAPK Pathways
• Share to Protein Tyrosine Phosphatases