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Publication Date:
July 2005
ISSN:
1437-4315
DOI:
10.1515/BC.2000.060

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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Ludwig, Stephan / Sies, Helmut / Stoffel, Markus / Turk, Boris / Wittinghofer, Alfred / Baumeister, Wolfgang / Bergeron, John / Bogyo, Matthew / Bürkle, Alexander / Cadenas, Enrique / Chiti, Fabrizio / Dikic, Ivan / Dobson, Christopher / Driessen, Arnold / Fritz, Hans / Gevaert, Kris / Hammann, Christian / Hartl, F. Ulrich / Häussinger, Dieter / Hiscott, John / Igarashi, Yasuyuki / Klotz, Lars-Oliver / Krüger, Achim / Magdolen, Viktor / Müschen, Markus / Narumiya, Shuh / Naumann, Michael / Pejler, Gunnar / Pfanner, Nikolaus / Pike, Robert / Potempa, Jan / Saftig, Paul / Sandhoff, Konrad / Schaffner, Walter / Sinning, Irmgard / Sommerhoff, Christian P.

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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: 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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