Insulin binding changes the interface region between .alpha. subunits of the insulin receptor
- 1 March 1989
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 28 (6) , 2722-2727
- https://doi.org/10.1021/bi00432a053
Abstract
The homobifunctional cross-linking reagent disuccinimidyl suberate (DSS) was used to probe the interface region between the two .alpha. subunits of the .alpha.2.beta.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.2 species was detected on protein blots from SDS gels using an anti-.alpha.-subunit antibody or 125I-concanavalin A. Alternatively, iodinated receptor was reacted with DSS and the .alpha.2 species measured directly in an SDS gel. As shown by all three assay systems, more .alpha.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 in response to insulin binding results in a change in the .alpha..sbd..alpha. interaction within the receptor complex. The results are consistent with a kinase activation mechanism involving communication between the two .alpha..beta. receptor halves.This publication has 65 references indexed in Scilit:
- Mechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding.Proceedings of the National Academy of Sciences, 1987
- An Mr 180000 protein is an endogenous substrate for the insulin-receptor-associated tyrosine kinase in human placentaBiochemical Journal, 1987
- Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody-stimulated glucose uptake and receptor kinase activity.Proceedings of the National Academy of Sciences, 1987
- Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucoseCell, 1986
- Urea treatment allows dithiothreitol to release the binding subunit of the insulin receptor from the cell membrane: Implications for the structural organization of the insulin receptorBiochemical and Biophysical Research Communications, 1985
- The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signallingCell, 1985
- Electrophoretic resolution of three major insulin receptor structures with unique subunit stoichiometries.Proceedings of the National Academy of Sciences, 1980
- Insulin receptor: covalent labeling and identification of subunits.Proceedings of the National Academy of Sciences, 1979
- [5] Direct identification of specific glycoproteins and antigens in sodium dodecyl sulfate gelsPublished by Elsevier ,1978
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970