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Buchner, Johannes

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred


SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751
Impact per Publication (IPP) 2015: 2.609

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ISSN
1437-4315
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Muscle Phosphorylase Kinase Is Not a Substrate of AMP-Activated Protein Kinase

A. Beyer / A. Kitzerow / B. Crute / B.E. Kemp / L.A. Witters / L.M.G. Heilmeyer jr

Citation Information: Biological Chemistry. Volume 381, Issue 5-6, Pages 457–461, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2000.060, July 2005

Publication History

Published Online:
2005-07-05

Abstract

AMP-activated protein kinase (AMPK) and cAMP-dependent protein kinase (cAMPK) have been reported to phosphorylate sites on phosphorylase kinase (PhK). Their target residues Ser 1018 and Ser 1020, respectively, are located in the so-called multi-phosphorylation domain in the PhK α subunit. In PhK preparations, only one of these serines is phosphorylated, but never both of them. The aim of this study was to determine whether phosphorylation by cAMPK or AMPK would influence subsequent phosphorylation by the other kinase. Surprisingly, employing four different PhK substrates, it could be demonstrated that, in contradiction to previous reports, PhK is not phosphorylated by AMPK.

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