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Phosphorylation of hepatic insulin receptor by casein kinase 2
Author(s) -
Grande Jorge,
Pérez Mercè,
Itarte Emilio
Publication year - 1988
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(88)80401-0
Subject(s) - phosphorylation , insulin receptor , chemistry , insulin receptor substrate , casein kinase 1 , casein kinase 2 , insulin , microbiology and biotechnology , medicine , endocrinology , biochemistry , protein kinase a , mitogen activated protein kinase kinase , biology , insulin resistance
Casein kinase 2 was able to phosphorylate the β‐subunit of hepatic insulin receptor in the presence of either ATP or GTP. Phosphorylation by casein kinase 2 was observed even in the absence of insulin, was inhibited by low heparin concentrations, and led to the incorporation of phosphate on serine and threonine residues. Casein kinase 2 phosphorylation of insulin receptor partially decreased its tyrosine kinase activity.