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Science 27 July 1990:
Vol. 249. no. 4967, pp. 408 - 411
DOI: 10.1126/science.2377895
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Articles

Science, Vol 249, Issue 4967, 408-411
Copyright © 1990 by American Association for the Advancement of Science

articles

Autophosphorylation of protein kinase C at three separated regions of its primary sequence

AJ Flint, RD Paladini, and DE Koshland Jr

Department of Molecular and Cellular Biology, University of California, Berkeley 94720.

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.


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A Unique Phosphorylation-dependent Mechanism for the Activation of Ca2+/Calmodulin-dependent Protein Kinase Type IV/GR.
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Protein Kinase C: Structure, Function, and Regulation.
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Determination of in Vivo Phosphorylation Sites in Protein Kinase C.
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Structural Basis for Species-specific Differences in the Phosphorylation of Na,K-ATPase by Protein Kinase C.
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Regulation of protein kinase Cbeta I by two protein-tyrosine kinases, Btk and Syk.
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Science. ISSN 0036-8075 (print), 1095-9203 (online)