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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 and L.M.G. Heilmeyer jr
Published/Copyright: July 5, 2005
Biological Chemistry
From the journal Volume 381 Issue 5-6

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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Published Online: 2005-07-05
Published in Print: 2000-06-21

Copyright © 2000 by Walter de Gruyter GmbH & Co. KG

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