APS, an adapter protein with a PH and SH2 domain, is a substrate for the insulin receptor kinase

Author:

AHMED Zamal12,SMITH Beverley J.1,KOTANI Kei2,WILDEN Peter3,PILLAY Tahir S.12

Affiliation:

1. Molecular Endocrinology Group, Institute of Cell Signalling and School of Biomedical Sciences, University of Nottingham Medical School, Queen's Medical Centre, Nottingham NG7 2UH, U.K.

2. Cell Signalling Laboratory, Department of Metabolic Medicine, Imperial College School of Medicine, Hammersmith Campus, 150 Du Cane Road, London W12 0NN, U.K.

3. Department of Pharmacology and the Molecular Biology Program, University of Missouri-Columbia, School of Medicine, One Hospital Drive, Columbia, MO 65212, U.S.A.

Abstract

APS (adapter protein with a PH and SH2 domain) is the newest member of a family of tyrosine kinase adapter proteins including SH2-B and Lnk. We previously identified SH2-B as an insulin-receptor-binding protein and substrate [Kotani, Wilden and Pillay (1998) Biochem J. 335, 103-109]. Here we show that APS interacts with the insulin receptor kinase activation loop through its SH2 domain and insulin stimulates the tyrosine-phosphorylation of APS. Furthermore, the phosphorylation of activation-loop tyrosine residues 1158 and 1162 are required for this interaction.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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