Interaction of the human insulin receptor with the ras oncogene product p21.

Autophosphorylation of the purified human insulin receptor tyrosyl kinase was found to be inhibited by the ras oncogene product p21 in a concentration- and GDP-dependent manner. GDP-beta-S but not Gpp(NH)p could substitute for GDP in eliciting the ras-dependent inhibition. The inhibition was seen with both normal or mutant (Lys-61) p21N-ras ...
and normal or mutant (Val-12) p21Ha-ras. Inhibition occurred at 23 degrees C but not 4 degrees C and was unaffected by the presence or absence of insulin although insulin stimulated the autophosphorylation rate of the receptor beta-subunit some 2-fold. The insulin receptor did not phosphorylate native p21Ha-ras in the presence or absence of added guanine nucleotide. After denaturation of p21Ha-ras with urea it became a substrate, but then failed to inhibit receptor autophosphorylation even in the presence of added GDP.
Mesh Terms:
GTP-Binding Proteins, Guanosine Diphosphate, Humans, Insulin, Phosphorylation, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins p21(ras), Receptor, Insulin, Recombinant Proteins
FEBS Lett.
Date: Jun. 15, 1987
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