Chutes and ladders: The search for protein kinases that act on AMPK

被引：100

作者：

Witters, LA ^{[1
]}

Kemp, BE

Means, AR

机构：

[1] Dartmouth Coll Sch Med, Dept Med, Hanover, NH 03755 USA

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

[3] Dartmouth Coll, Dept Biol Sci, Hanover, NH 03755 USA

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

[5] CSIRO Mol & Hlth Technol, Parkville, Vic 3052, Australia

[6] Duke Univ, Dept Pharmacol & Canc Biol, Durham, NC 27710 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2006年 / 31卷 / 01期

关键词：

D O I：

10.1016/j.tibs.2005.11.009

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), a key regulator of energy homeostasis in mammalian cells, is, in turn, regulated by long-sought upstream protein kinases (AMPKs). Following the recent identification of the tumor-suppressor kinase LIKB1 as an AMPKK, a broader role for AMPK in metabolic economy has been unveiled by a new body of work from three groups that implicates the Ca2+/calmodulin-dependent protein kinase kinases as AMPKKs. We suggest that PIKE (protein kinase 'energy' or 'economy') is now an apt name for this kinase, which regulates both cellular and whole-organism energy homeostasis.

引用

页码：13 / 16

页数：4

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