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IGF1 — PMPCB

Text-mined interactions from Literome

Xi et al., Mol Endocrinol 2008 : Our previous studies have indicated an essential role of p52shc in mediating IGF-I activation of MAPK in smooth muscle cells ( SMC ) ... Knockdown p66shc by small interfering RNA enhanced IGF-I stimulated p52shc tyrosine phosphorylation and growth factor receptor bound protein-2 ( Grb2 ) association, resulting in increased IGF-I dependent MAPK activation ... Overexpression of p66shc impaired IGF-I stimulated p52shc tyrosine phosphorylation and p52shc-Grb2 association ... These findings indicate that p66shc functions to negatively regulate the formation of a signaling complex that is required for p52shc activation in response to IGF-I , thus leading to attenuation of IGF-I stimulated cell proliferation and migration
Xi et al., J Biol Chem 2010 : Disruption of this interaction using a synthetic peptide containing the p66 ( shc ) polyproline domain or expression of a p66 ( shc ) mutant containing substitutions for the proline residues ( P47A/P48A/P50A ) resulted in enhanced Src kinase activity, p52 ( shc ) phosphorylation, MAPK activation, and cell proliferation in response to IGF-I
Tartare-Deckert et al., J Biol Chem 1995 : Our findings can be summarized as follows : ( i ) the tyrosine kinase activity of the IGF-IR is essential for the interaction with p52Shc and IRS-1, ( ii ) p52Shc and IRS-1 bind to the IGF-IR in the NPEY-juxtamembrane motif, ( iii ) contrary to p52Shc, IRS-1 binds also to the major autophosphorylation sites ( Tyr-1131, -1135, and -1136 ) of the IGF-IR, and ( iv ) the amino-terminal domain of p52Shc is required for its association with the IR and the IGF-IR