Literature DB >> 17705797

The AMP-activated protein kinase: more than an energy sensor.

Louis Hue1, Mark H Rider.   

Abstract

The AMPK (AMP-activated protein kinase) is a highly conserved eukaryotic protein serine/threonine kinase. It mediates a nutrient signalling pathway that senses cellular energy status and was appropriately called the fuel gauge of the cell. At the cellular level, AMPK controls energy homoeostasis by switching on catabolic ATP-generating pathways, while switching off anabolic ATP-consuming processes. Its effect on energy balance extends to whole-body energy homoeostasis, because, in the hypothalamus, it integrates nutritional and hormonal signals that control food intake and body weight. The interest in AMPK also stems from the demonstration of its insulin-independent stimulation of glucose transport in skeletal muscle during exercise. Moreover, the potential importance of AMPK in metabolic diseases is supported by the notion that AMPK mediates the anti-diabetic action of biguanides and thiazolidinediones and that it might be involved in the metabolic syndrome. Finally, the more recent demonstration that AMPK activation could occur independently of changes in cellular energy status, suggests that AMPK action extends to the control of non-metabolic functions.

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Year:  2007        PMID: 17705797     DOI: 10.1042/BSE0430121

Source DB:  PubMed          Journal:  Essays Biochem        ISSN: 0071-1365            Impact factor:   8.000


  28 in total

1.  AMPK isoform expression in the normal and failing hearts.

Authors:  Maengjo Kim; Mei Shen; Soeun Ngoy; Georgios Karamanlidis; Ronglih Liao; Rong Tian
Journal:  J Mol Cell Cardiol       Date:  2012-01-31       Impact factor: 5.000

Review 2.  Role of AMP-activated protein kinase in metabolic depression in animals.

Authors:  Mark H Rider
Journal:  J Comp Physiol B       Date:  2015-07-15       Impact factor: 2.200

3.  Stimulation of human and mouse erythrocyte Na(+)-K(+)-2Cl(-) cotransport by osmotic shrinkage does not involve AMP-activated protein kinase, but is associated with STE20/SPS1-related proline/alanine-rich kinase activation.

Authors:  Brice Sid; Lisa Miranda; Didier Vertommen; Benoît Viollet; Mark H Rider
Journal:  J Physiol       Date:  2010-05-04       Impact factor: 5.182

4.  AMPKα2 Protects Against the Development of Heart Failure by Enhancing Mitophagy via PINK1 Phosphorylation.

Authors:  Bei Wang; Jiali Nie; Lujin Wu; Yangyang Hu; Zheng Wen; Lingli Dong; Ming-Hui Zou; Chen Chen; Dao Wen Wang
Journal:  Circ Res       Date:  2017-12-28       Impact factor: 17.367

5.  Fyn-dependent regulation of energy expenditure and body weight is mediated by tyrosine phosphorylation of LKB1.

Authors:  Eijiro Yamada; Jeffrey E Pessin; Irwin J Kurland; Gary J Schwartz; Claire C Bastie
Journal:  Cell Metab       Date:  2010-02-03       Impact factor: 27.287

6.  PKA phosphorylates and inactivates AMPKalpha to promote efficient lipolysis.

Authors:  Nabil Djouder; Roland D Tuerk; Marianne Suter; Paolo Salvioni; Ramon F Thali; Roland Scholz; Kari Vaahtomeri; Yolanda Auchli; Helene Rechsteiner; René A Brunisholz; Benoit Viollet; Tomi P Mäkelä; Theo Wallimann; Dietbert Neumann; Wilhelm Krek
Journal:  EMBO J       Date:  2009-11-26       Impact factor: 11.598

7.  Phosphorylation of translation factors in response to anoxia in turtles, Trachemys scripta elegans: role of the AMP-activated protein kinase and target of rapamycin signalling pathways.

Authors:  Mark H Rider; Nusrat Hussain; Stephen M Dilworth; Kenneth B Storey
Journal:  Mol Cell Biochem       Date:  2009-07-05       Impact factor: 3.396

Review 8.  The Randle cycle revisited: a new head for an old hat.

Authors:  Louis Hue; Heinrich Taegtmeyer
Journal:  Am J Physiol Endocrinol Metab       Date:  2009-06-16       Impact factor: 4.310

9.  The regulation of AMPK signaling in a natural state of profound metabolic rate depression.

Authors:  Christopher J Ramnanan; David C McMullen; Amy G Groom; Kenneth B Storey
Journal:  Mol Cell Biochem       Date:  2009-09-15       Impact factor: 3.396

10.  Interaction of the WD40 domain of a myoinositol polyphosphate 5-phosphatase with SnRK1 links inositol, sugar, and stress signaling.

Authors:  Elitsa A Ananieva; Glenda E Gillaspy; Amanda Ely; Ryan N Burnette; F Les Erickson
Journal:  Plant Physiol       Date:  2008-10-17       Impact factor: 8.340

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