Insulin-stimulated phosphorylation of the insulin receptor precursor |
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Authors: | R W Rees-Jones J A Hedo Y Zick J Roth |
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Institution: | Diabetes Branch, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20205 USA |
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Abstract: | The alpha and beta subunits of the insulin receptor, Mr = 135K and 95K, appear to be synthesized via a single polypeptide precursor of Mr = 190K. We have investigated whether insulin stimulates the phosphorylation of this proreceptor, as is the case with mature receptor. Rat liver endoplasmic reticulum membranes were solubilized in Triton X-100 and chromatographed sequentially on wheat-germ agglutinin-agarose and lentil lectin-agarose columns. Phosphorylation of the lentil eluate with gamma 32P]ATP revealed an insulin-stimulated phosphoprotein of Mr = 192K, which was recognized by antireceptor antibody, compatible with the receptor precursor. This suggests that further processing of the Mr = 190K insulin receptor precursor is not necessary for insulin binding, kinase activation, and receptor phosphorylation. |
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