Article
Phosphorylation state and biological function of a mutant human insulin receptor Val996.
The Journal of biological chemistry - 5 Sept 1990
Yamamoto-Honda R, Koshio O, Tobe K, Shibasaki Y, Momomura K, Odawara M, Kadowaki T, Takaku F, Akanuma Y, Kasuga M
Abstract excerpt
Chinese hamster ovary (CHO) cell transfectants that expressed human insulin receptors whose glycine 996 was substituted by valine were studied. Receptor processing and insulin binding were unaffected by this mutation; however, this mutant insulin receptor had little or no tyrosine kinase activity. Nevertheless, the Val996 mutant exhibited seryl and threonyl phosphorylation in both the basal and insulin-stimulated...
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