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Science 15 November 1985:
Vol. 230. no. 4727, pp. 827 - 829
DOI: 10.1126/science.3904001
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Articles

Science, Vol 230, Issue 4727, 827-829
Copyright © 1985 by American Association for the Advancement of Science

articles

The insulin receptor contains a calmodulin-binding domain

CB Graves, RR Goewert, and JM McDonald

Substantial evidence suggests that calcium has a pivotal role in regulating the initial events through which insulin alters plasma membrane metabolism. Because binding of insulin to its receptor represents the initial site of insulin action in the plasma membrane, studies were undertaken to determine whether the insulin receptor is a calmodulin-binding protein. Preparations enriched in the insulin receptor and calmodulin-binding proteins were isolated from detergent-solubilized rat adipocyte membranes by chromatography with wheat germ agglutinin agarose and calmodulin-conjugated Sepharose, respectively. Substantial purification of a manganese-dependent, insulin-sensitive phosphoprotein of 95K identified as the beta subunit of the insulin receptor was accomplished. Binding and photocovalent cross-linking of iodine-125-labeled calmodulin to these affinity-purified preparations and to isolated plasma membranes, followed by immunoadsorption with insulin receptor antibodies bound to protein A Sepharose, resulted in significant purification of a binding complex of 110K to 140K. These results indicate that the adipocyte insulin receptor or a polypeptide closely associated with the receptor is a calmodulin-binding protein.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Interaction of Calmodulin, a Sorting Nexin and Kinase-Associated Protein Phosphatase with the Brassica oleracea S Locus Receptor Kinase.
V. Vanoosthuyse, G. Tichtinsky, C. Dumas, T. Gaude, and J. M. Cock (2003)
Plant Physiology 133, 919-929
   Abstract »    Full Text »    PDF »
Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III.
J. Affholter, V. Fried, and R. Roth (1988)
Science 242, 1415-1418
   Abstract »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)