Article
Mutation of arginine 86 to proline in the insulin receptor alpha subunit causes lack of transport of the receptor to the plasma membrane, loss of binding affinity and a constitutively activated tyrosine kinase in transfected cells.
Biochemical and biophysical research communications - 30 Apr 1993
Grønskov K, Vissing H, Shymko R M, Tornqvist H, De Meyts P
Abstract excerpt
We have investigated the role of Ser 85 and Arg 86 of the human insulin receptor (HIR) in insulin binding and tyrosine kinase activity by mutational analysis. Four mutant cDNAs were created (R86P, R86N, S85T+R86N, S85W+R86K) and stably transfected into BHK cells. R86P-HIR was also transiently exp...
Topics
- Animals
- Arginine
- Binding Sites
- Biological Transport
- Cell Membrane
- Cells, Cultured
- Cricetinae
- Enzyme Activation
- Humans
- Immunohistochemistry
- Mutation