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Administration of insulin to rats caused a transient increase in the amount of hepatic insulin receptor present in clathrin-coated vesicles and endosomes. However, the total 'in vitro' insulin stimulated tyrosine kinase activity of the receptor present in endosomes did not vary when expressed per mg of protein and decreased when expressed per β-subunit content. A decrease in the endogenous phospho...
The αβ heterodimeric form of untreated hepatic insulin receptor was a substrate for casein kinase 2, whereas the α 2 β 2 heterotetramer was not. On the contrary, autophosphorylation was detected only in the heterotetramer. Dissociation of the receptor by treatment with dithiothreitol decreased its autophosphorylation but favoured phosphorylation of its β-subunit by casein kinase 2.
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