New paper linking SHP2 phosphatase to RET signaling out in the JBC

Our latest paper has been made available today at the Papers In Press site of the Journal of Biological Chemistry (Perrinjaquet et al. JBC 2010). This work identifies the protein tyrosine phosphatase SHP2 as a novel direct interactor of the receptor tyrosine kinase RET. SHP2 is the first effector known to bind to phosphorylated Tyr687 in the juxtamembrane region of the receptor. SHP2 recruitment contributes to the ability of RET to activate the PI3K/AKT pathway and promote survival and neurite outgrowth in primary neurons. Together with other findings, this work establishes SHP2 as a novel positive regulator of the neurotrophic activities of RET, and reveal Tyr687 as a critical platform for integration of RET signals. We anticipate that several other phospho-tyrosines of unknown function in neuronal receptor tyrosine kinases will also support similar regulatory functions. Read the full paper HERE.