HSP70 binds to SHP2 and has effects on the SHP2-related EGFR/GAB1 signaling pathway.

ABSTRACT: The Src homology phosphotyrosyl phosphatase, SHP2, is a positive effector of EGFR signaling. However, the molecular mechanism and biological functions of SHP2 regulation are still not completely known. To better understand the cellular processes in which SHP2 participates, we carried out mass spectrometry to find SHP2 binding proteins. FLAG-SHP2 complexes were isolated by affinity purification, and associated proteins were identified by in-gel trypsin digestion followed by LC/MS/MS mass spectrometry. Among the identified proteins, we focus in this report on the heat shock protein 70 (HSP70). Physical interactions of SHP2 with HSP70 were confirmed in vivo. Further experiments demonstrate that EGF does not activate binding of SHP2 with HSP70 rather the binding appears to be constitutive. How

SUBMITTER: Yoo JC 

PROVIDER: S-EPMC1698467 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature