Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain |
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| Authors: | Keats Nelms Thomas J. O'Neill Shiqing Li Stevan R. Hubbard Thomas A. Gustafson William E. Paul |
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| Affiliation: | (1) Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA, US;(2) Department of Physiology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA, US;(3) Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University Medical Center, 540 First Avenue, New York, New York 10016, USA, US;(4) Metabolex, Inc., 3876 Bay Center Place, Hayward, California 94545, USA, US |
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| Abstract: | The SH2-B protein is an SH2-domain-containing molecule that interacts with a number of phosphorylated kinase and receptor molecules including the insulin receptor. Two isoforms of the SH2-B have been identified and have been proposed to arise through alternate splicing. Here we have identified a third isoform of the SH2-B protein, SH2-Bγ, that interacts specifically with the insulin receptor. This interaction required phosphorylation of residue Y1146 in the triple tyrosine motif within the activation loop of the IR kinase and is one of only two signaling molecules shown to interact directly with this residue of the insulin receptor kinase domain. The intron/exon structure of the SH2-B gene was determined. Alternate splice sites utilized to generate the different isoforms of the SH2-B protein were identified in the 3′ end of the SH2-B gene immediately downstream of the exon encoding the core of the SH2 domain. Additionally, the chromosomal location of the SH2-B gene was determined to be the distal arm of mouse Chromosome (Chr) 7 in a region linked to obesity in mice. Received: 13 May 1999 / Accepted: 13 August 1999 |
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