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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.

Authors
  • O'Brien, R
  • Houslay, M D
  • Brindle, N P
  • Milligan, G
  • Whittaker, J
  • Siddle, K
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Feb 15, 1989
Volume
158
Issue
3
Pages
743–748
Identifiers
PMID: 2465763
Source
Medline
License
Unknown

Abstract

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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