Autophosphorylation of Protein Kinase C at Three Separated Regions of Its Primary Sequence
- 27 July 1990
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 249 (4967) , 408-411
- https://doi.org/10.1126/science.2377895
Abstract
The major autophosphorylation sites of the rat beta II isozyme of protein kinase C were identified. The modified threonine and serine residues were found in the amino-terminal peptide, the carboxyl-terminal tail, and the hinge region between the regulatory lipid-binding domain and the catalytic kinase domain. Because this autophosphorylation follows an intrapeptide mechanism, extraordinary flexibility of the protein is necessary to phosphorylate the three regions. Comparison of the sequences surrounding the modified residues showed no obvious recognition motif nor any similarity to substrate phosphorylation sites, suggesting that proximity to the active site may be the primary criterion for their phosphorylation.This publication has 32 references indexed in Scilit:
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