Identification of a phosphorylation site of the rat insulin receptor catalyzed by protein kinase C in an intact cell

FEBS Letters
O KoshioM Kasuga

Abstract

In two-dimensional tryptic phosphopeptide mapping, the beta-subunit of the insulin receptor phosphorylated by 12-O-tetradecanoylphorbol-13-acetate in rat hepatoma cells (H-35) was separated into one phosphothreonine-containing peptide and several phosphoserine-containing peptides. The synthetic peptide coding residues 1327-1343 in the C-terminal region of the rat insulin receptor was phosphorylated at the threonine residue by protein kinase C in a phosphatidylserine and oleoylacetylglycerol dependent manner. Tryptic digest of this phosphopeptide migrated to the same position as the phosphothreonine containing peptide obtained from the beta-subunit in two-dimensional phosphopeptide mapping. These data suggested that Thr 1336 of the insulin receptor is the site of phosphorylation by protein kinase C in intact cells.

References

Jan 1, 1983·Methods in Enzymology·J A CooperT Hunter
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Dec 1, 1984·Proceedings of the National Academy of Sciences of the United States of America·S TakayamaC R Kahn

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Citations

May 1, 1993·Journal of Cellular Biochemistry·R V Considine, J F Caro
Jan 1, 1990·The International Journal of Biochemistry·T O'Hare, P F Pilch
Jan 1, 1991·Cellular Signalling·G Grunberger
Mar 30, 2002·Molecular Endocrinology·Michael LeitgesMichael Letiges
May 30, 2020·Lipids in Health and Disease·Katarzyna KolczynskaGrzegorz Sumara
May 1, 1991·Biochemical Pharmacology·J M Backer, G L King
Aug 1, 1991·Metabolism: Clinical and Experimental·K NagyG Grunberger
Dec 31, 1991·Biochemical and Biophysical Research Communications·D Müller-WielandC R Kahn

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