Protein Kinase C Directly Phosphorylates the Insulin Receptor in vitro and Reduces Its Protein-Tyrosine Kinase Activity

The β subunit of purified insulin receptor is phosphorylated on a serine residue by purified preparations of protein kinase C (ATP: protein phosphotransferase, EC 2.7.1.37). This phosphorylation is inhibited by antibodies to protein kinase C and stimulated by phospholipids, diacylglycerol, and Ca2+....

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1986-08, Vol.83 (16), p.5822-5824
Main Authors: Bollag, Gideon E., Roth, Richard A., Beaudoin, Jacqueline, Mochly-Rosen, Daria, Koshland, Daniel E.
Format: Article
Language:English
Subjects:
Animals
Antibodies
Biochemistry
Chromatography
Enzyme Activation
Insulin
Insulin - analogs & derivatives
Insulin - metabolism
Kinetics
Macromolecular Substances
Monoclonal antibodies
Phorbol esters
Phosphatidylserines
Phosphoamino acids
Phosphorylation
protein kinase C
Protein Kinase C - metabolism
Protein-Tyrosine Kinases - metabolism
Receptor, Insulin - metabolism
Receptors
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Summary:The β subunit of purified insulin receptor is phosphorylated on a serine residue by purified preparations of protein kinase C (ATP: protein phosphotransferase, EC 2.7.1.37). This phosphorylation is inhibited by antibodies to protein kinase C and stimulated by phospholipids, diacylglycerol, and Ca2+. The phosphorylation of the receptor by protein kinase C does not affect its insulin-binding activity but does inhibit by 65% the receptor's intrinsic tyrosine-specific protein kinase activity (ATP: protein-tyrosine O-phosphotransferase, EC 2.7.1.112). These results indicate that activators of protein kinase C, such as phorbol esters, desensitize cells to insulin by direct protein kinase C action on the insulin receptor.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.83.16.5822