期刊
FEBS LETTERS
卷 493, 期 2-3, 页码 106-111出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(01)02282-7
关键词
Grb10; insulin receptor; insulin-like growth factor 1 receptor; receptor tyrosine kinase; enzyme inhibition
资金
- NIDDK NIH HHS [DK52916] Funding Source: Medline
Grb7, Grb10 and Grb14 comprise a family of adaptor proteins that interact with numerous receptor tyrosine kinases upon receptor activation. Between the pleckstrin homology (PH) domain and the Src homology 2 (SH2) domain of these proteins is a region of approximately 50 residues known as the BPS (between PH and SH2) domain. Here we show, using purified recombinant proteins, that the BPS domain of Grb10 directly inhibits substrate phosphorylation by the activated tyrosine kinase domains of the insulin receptor and the insulin-like growth factor I (IGF1) receptor, although inhibition by the BPS domain is dependent on tyrosine phosphorylation of;he kinase activation loop, peptide competition experiments indicate that the BPS domain does not bind directly to phosphotyrosine. These studies pro, ide a molecular mechanism by which Grb10 functions as a negative regulator of insulin- and/or IGF1-mediated signaling, (C) 2001 Published by Elsevier Science B,V, on behalf of the Federation of European Biochemical Societies.
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