Author(s)

Xiaochen Lin, Olga Vinogradova

Department of Pharmaceutical Sciences, School of Pharmacy, University of Connecticut at Storrs, Storrs, USA.

The Shc adaptor protein, particularly its p52 isoform, has been identified as a primary signaling partner for the tyrosine(s)-phosphorylated cytoplasmic tails of activated β₃ integrins. Inspired by our recent structure of the Shc PTB domain in complex with a bi-phosphorylated peptide derived from β₃ cytoplasmic tail, we have initiated the investigation of Shc interaction with phospholipids of the membrane. We are particularly focused on PtdIns and their effects on Shc mediated integrin signaling in vitro. Here we present thermodynamic profiles and molecular details of the interactions between Shc, integrin, and PtdIns, all of which have been studied by ITC and solution NMR methods. A model of p52 Shc interaction with phosphorylated β₃ integrin cytoplasmic tail at the cytosolic face of the plasma membrane is proposed based on these data.

Shc, Integrin, Phosphatidylinositol, ITC, NMR

Lin, X. and Vinogradova, O. (2015) Phospho-Tyrosine(s) vs. Phosphatidylinositol Binding in Shc Mediated Integrin Signaling. American Journal of Molecular Biology, 5, 17-31. doi: 10.4236/ajmb.2015.52003.