Muscle phosphorylase kinase is not a substrate of AMP-activated protein kinase

被引：17

作者：

Beyer, A

Kitzerow, A

Crute, B

Kemp, BE

Witters, LA

Heilmeryer, LMG

机构：

[1] Ruhr Univ Bochum, Inst Physiol Chem, D-44780 Bochum, Germany

[2] Dartmouth Med Sch, Dept Med, Hanover, NH 03755 USA

[3] Dartmouth Med Sch, Dept Biochem, Hanover, NH 03755 USA

[4] St Vincents Inst Med Res, Fitzroy, Vic 3065, Australia

来源：

BIOLOGICAL CHEMISTRY | 2000年 / 381卷 / 5-6期

关键词：

AMP-activated protein kinase; cAMP-dependent protein kinase; multi-phosphorylation domain; phosphorylase kinase;

D O I：

10.1515/BC.2000.060

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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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页码：457 / 461

页数：5

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