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Insulin binding changes the interface region between. alpha. subunits of the insulin receptor

Journal Article · · Biochemistry; (USA)
DOI:https://doi.org/10.1021/bi00432a053· OSTI ID:5546924
;  [1]
  1. Boston Univ. School of Medicine, MA (USA)
The homobifunctional cross-linking reagent disuccinimidyl suberate (DSS) was used to probe the interface region between the two {alpha} subunits of the {alpha}{sub 2}{beta}{sub 2} human insulin receptor. The two {alpha} subunits formed a covalent dimer when affinity-purified receptor or membrane-bound receptor was reacted with DSS. The {alpha}{sub 2} species was detected on protein blots from SDS gels using an anti-{alpha}-subunit antibody or {sup 125}I-concanavalin A. Alternatively, iodinated receptor was reacted with DSS and the {alpha}{sub 2} species measured directly in an SDS gel. As shown by all three assay systems, more {alpha}{sub 2} was formed when insulin was bound to receptor than when insulin was absent. These data indicate that the conformational change which occurs in the {alpha} subunit response to insulin binding results in a change in the {alpha}-{alpha} interaction within the receptor complex. The results are consistent with a kinase activation mechanism involving communication between the two {alpha}{beta} receptor halves.
OSTI ID:
5546924
Journal Information:
Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 28:6; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English