Skip to Main content Skip to Navigation
Journal articles

Bypassing AMPK Phosphorylation

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.
Keywords : AMPK
Document type :
Journal articles
Complete list of metadatas

Cited literature [9 references]  Display  Hide  Download

https://www.hal.inserm.fr/inserm-01171798
Contributor : Benoit Viollet <>
Submitted on : Monday, July 6, 2015 - 1:07:00 PM
Last modification on : Wednesday, July 15, 2020 - 9:10:04 AM
Long-term archiving on: : Tuesday, April 25, 2017 - 11:51:22 PM

Files

Preview_Chem_Biol_Oakhill2014_...
Files produced by the author(s)

Identifiers

Collections

Citation

Benoit Viollet, Marc Foretz, Uwe Schlattner. Bypassing AMPK Phosphorylation. Chemistry and Biology, Elsevier, 2014, 21 (5), pp.567-569. ⟨10.1016/j.chembiol.2014.05.003⟩. ⟨inserm-01171798⟩

Share

Metrics

Record views

459

Files downloads

1054