期刊
BIOLOGICAL CHEMISTRY
卷 381, 期 5-6, 页码 457-461出版社
WALTER DE GRUYTER & CO
DOI: 10.1515/BC.2000.060
关键词
AMP-activated protein kinase; cAMP-dependent protein kinase; multi-phosphorylation domain; phosphorylase kinase
资金
- NIDDK NIH HHS [DK35712] Funding Source: Medline
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 alpha 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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