Elucidation of the quaternary structure of the insulin receptor

Abstract

Photoreactive insulin analogues specifically label predominantly one polypeptide in the insulin receptor of rat liver plasma membranes. We have used the bifunctional reagent disuccinimidyl suberate to cross-link this polypeptide to its neighbouring, but not necessarily labelled, subunits. The results of these studies show that (1) there are at least three types of subunit in the receptor, with apparent Mr (Mapp.) values of 65 000, 95 000 and 120 000; (2) the receptor appears to consist of two Mapp. 120 000, one Mapp. 95 000 and one Mapp. 65 000 subunits; (3) the Mapp. 65 000 subunit, which has not been previously reported, may be only loosely attached to the receptor, and does not interact directly with the insulin-binding subunit (M app. 120 000).