Muscle Phosphorylase Kinase Is Not a Substrate of AMP-Activated Protein Kinase
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A. Beyer
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.
Copyright © 2000 by Walter de Gruyter GmbH & Co. KG
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- Highlight: GTP Binding Proteins Central Regulators in Cell Biology
- Signal Transduction and Post-Transcriptional Gene Expression
- Regulation of GTPases in the Bacterial Translation Machinery
- GTPase Mechanisms and Functions of Translation Factors on the Ribosome
- The Role of Heterotrimeric G Proteins in Platelet Activation
- Upstream and Downstream of Ran GTPase
- Nogo-A, a Potent Inhibitor of Neurite Outgrowth and Regeneration
- Rho GTPases as Targets of Bacterial Protein Toxins
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