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J Biol Chem, Vol. 273, Issue 47, 31061-31067, November 20, 1998

IRS Pleckstrin Homology Domains Bind to Acidic Motifs in Proteins

Deborah J. BurksDagger , Jian Wang, Heather ToweryDagger , Osamu Ishibashiparallel , Douglas LoweDagger , Heimo Riedel, and Morris F. WhiteDagger

From the Dagger  Howard Hughes Medical Institute, Joslin Diabetes Center, Harvard Medical School, Boston, Massachusetts 02215, the  Department of Biological Sciences and Karmanos Cancer Institute, Wayne State School of Medicine, Detroit Michigan 48202, and the parallel  First Department of Medicine, Toyama Medical and Pharmacology University, Toyama 930-01, Japan

Using a yeast two-hybrid system, we identified several proteins that interact with the PH domains in IRS-1 and IRS-2, including Lon protease, myeloblast protein, and nucleolin. Although the roles of these molecules in insulin action are not yet known, each protein contained an acidic motif that interacted with the PH domain of IRS-2. However, only the acidic motif in nucleolin bound to IRS-1, suggesting that the PH domain in IRS-1 and IRS-2 are not identical. Moreover, synthetic peptides based on the acidic motif in Lon protease and myeloblast protein inhibited the binding of nucleolin to the PH domain of IRS-2 but not to the PH domain of IRS-1, confirming the selectivity of these PH domains. The ability to bind acidic motifs may be a specific function of the PH domain in IRS proteins, because the PH domains in beta ARK, phospholipase Cgamma , or spectrin did not bind nucleolin. In 32D cells, nucleolin bound to both IRS-1 and IRS-2, and expression of the acidic motif of nucleolin inhibited insulin-stimulated tyrosine phosphorylation of IRS-1 and IRS-2. These results suggest that the binding of acidic motifs to the PH domain of IRS-1 and IRS-2 disrupts coupling to the activated insulin receptor. Our results are consistent with the hypothesis that the PH domain in the IRS proteins may ordinarily bind acidic peptide motifs in membrane proteins or other acidic membrane elements that couple IRS proteins to activated membrane receptors.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.


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