Binding to GDP-agarose identifies a novel 60kDa substrate for the insulin receptor tyrosyl kinase in mouse NIH-3T3 cells expressing high concentrations of the human insulin receptor

Biochemical and Biophysical Research Communications
R M O'BrienK Siddle


Insulin increased dramatically the tyrosyl phosphorylation of the insulin receptor beta-subunit in mouse NIH-3T3 fibroblasts transfected with the human insulin receptor. Insulin also increased the phosphorylation, on tyrosine residues, of an endogenous 60kDa protein. This protein was identified after being eluted from a GDP-agarose support by GDP. It is suggested that the 60kDa species may be a novel guanine nucleotide binding protein which is specifically phosphorylated by the insulin receptor.


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Aug 31, 1990·Biochemical and Biophysical Research Communications·H W Davis, J M McDonald
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