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Science 5 December 1980:
Vol. 210. no. 4474, pp. 1152 - 1153
DOI: 10.1126/science.7003712
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Articles

Science, Vol 210, Issue 4474, 1152-1153
Copyright © 1980 by American Association for the Advancement of Science

articles

Hormone binding alters the conformation of the insulin receptor

PF Pilch and MP Czech

Fat cells or fat cell membranes were briefly subjected to mild proteolysis under conditions where insulin receptors were either free or bound to (125)I-labeled insulin. When receptors were then affinity-labeled to visualize the effects of this treatment, it was observed that receptors that had been occupied by ligand during proteolysis exhibited greater rates of degradation than unoccupied receptors. These results demonstrate that insulin-receptor interaction induces a change in receptor structure that may be related to signal transmission.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Hyperphosphorylation of MEF2A in primary adipocytes correlates with downregulation of human GLUT4 gene promoter activity.
D. P. Sparling, B. A. Griesel, and A. L. Olson (2007)
Am J Physiol Endocrinol Metab 292, E1149-E1156
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