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Insulin binds to and promotes the phosphorylation of a M r 210 000 component of its receptor in detergent extracts of rat liver microsomes
Author(s) -
Blackshear Perry J.,
Nemenoff Raphael A.,
Avruch Joseph
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80587-0
Subject(s) - phosphorylation , insulin receptor , tyrosine , insulin , biochemistry , tyrosine phosphorylation , immunoprecipitation , biology , insulin receptor substrate , chemistry , endocrinology , insulin resistance , gene
Insulin in the presence of Mn 2+ and [γ 32 P]ATP promoted the phosphorylation of two proteins of M r 95 000 and M r 210 000 in detergent extracts of rat liver microsomes. The M r 210 000 protein was identified as a component of the insulin receptor by immunoprecipitation. It also bound [ 125 I]insulin specifically, was phosphorylated largely on a tyrosine residue and could not be cleaved to smaller subunits under extreme reducing conditions. The M r 210 000 protein appears to be a component of a sub‐population of liver membrane insulin receptors in which insulin‐binding and insulin‐stimulated tyrosine kinase phosphorylation site(s) reside in a single polypeptide chain.