Conformational states of the insulin receptor.
Insulin binding to the alpha-subunit of the purified insulin receptor changed the interaction between beta-subunits. This conformational change was demonstrated after labeling the receptor's beta-subunit by autophosphorylation in the absence of insulin, and then crosslinking the subunits to each other with bis (sulfosuccinimidyl) suberate. The convalent oligomers were resolved by reduction and denaturing gel electrophoresis. Insulin increased the rate of crosslinking, especially the formation of beta-beta dimers. These results support a conformational change following insulin binding, and may reflect the insulin-induced activation of autophosphorylation.
Schenker
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Department of Biochemistry, Mount Sinai School of Medicine, New York, New York 10029.
Kohanski
R A
RA
D000818:Animals; D003432:Cross-Linking Reagents; D066298:In Vitro Techniques; D007328:Insulin / Q000378:metabolism*; D051379:Mice; D010766:Phosphorylation; D011487:Protein Conformation; D011972:Receptor, Insulin / Q000378:metabolism / Q000648:ultrastructure*; D013997:Time Factors
D003432:Cross-Linking Reagents; D007328:Insulin; D011972:Receptor, Insulin