Bypassing AMPK phosphorylation

Benoit Viollet; Marc Foretz; Uwe Schlattner

doi:10.1016/j.chembiol.2014.05.003

Bypassing AMPK phosphorylation

Chem Biol. 2014 May 22;21(5):567-9. doi: 10.1016/j.chembiol.2014.05.003.

Authors

Benoit Viollet¹, Marc Foretz², Uwe Schlattner³

Affiliations

¹ INSERM, U1016, Institut Cochin, 75014 Paris, France; CNRS, UMR8104, 75014 Paris, France; Université Paris Descartes, Sorbonne Paris Cité, 75006 Paris, France. Electronic address: [email protected].
² INSERM, U1016, Institut Cochin, 75014 Paris, France; CNRS, UMR8104, 75014 Paris, France; Université Paris Descartes, Sorbonne Paris Cité, 75006 Paris, France.
³ Laboratory of Fundamental and Applied Bioenergetics, University Grenoble Alpes, 38185 Grenoble, France; Inserm, U1055, 38041 Grenoble, France.

PMID: 24856137
DOI: 10.1016/j.chembiol.2014.05.003

Abstract

AMP-activated protein kinase (AMPK) functions as a signaling hub to balance energy supply with demand. Phosphorylation of activation loop Thr172 has been considered as an essential step in AMPK activation. In this issue of Chemistry & Biology, Scott and colleagues show that the small molecule direct AMPK activator, A-769662, bypasses this phosphorylation event and acts synergistically with AMP on naive AMPK.

Publication types

Comment

MeSH terms

AMP-Activated Protein Kinases / metabolism*
Adenosine Monophosphate / pharmacology*
Animals
Biphenyl Compounds
Pyrones / pharmacology*
Signal Transduction*
Thiophenes / pharmacology*

Substances

Biphenyl Compounds
Pyrones
Thiophenes
Adenosine Monophosphate
AMP-Activated Protein Kinases
4-hydroxy-3-(4-(2-hydroxyphenyl)phenyl)-6-oxo-7H-thieno(2,3-b)pyridine-5-carbonitrile