Journal
FEBS JOURNAL
Volume 280, Issue 16, Pages 3723-3733Publisher
WILEY
DOI: 10.1111/febs.12364
Keywords
activators; AMP-activated protein kinase; carbohydrate-binding module; heterotrimeric complex; myristoylation; phosphorylation; posttranslational modification; structural analysis; sumoylation; ubiquitination
Categories
Funding
- Spanish Ministry of Education and Science [SAF2011-27442]
- Generalitat Valenciana [Prometeo 2009/051]
- Spanish Research Council (CSIC)
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AMP-activated protein kinase (AMPK) is a sensor of energy status composed of a catalytic subunit (AMPK), a scaffolding subunit (AMPK) and a regulatory subunit involved in nucleotide binding (AMPK). Activation of AMPK results in enhancement of catabolic processes and downregulation of anabolic pathways with the aim to equilibrate the energy status of the cell. AMPK complex has been traditionally focused on modifications of AMPK and AMPK subunits by post-translational changes (i.e. phosphorylation of the catalytic subunit) and allosteric activation by AMP. In this review, we summarize recent reports that indicate that AMPK subunits are also critical players in AMPK function, because they can regulate the phosphorylation status and activity of the AMPK complex. AMPK1- and AMPK2-containing complexes differ in their capacity to be activated by specific drugs (i.e. A769622, salicylate) and also by the ability to undergo post-translational modifications. AMPK complexes containing specific beta-isoforms.
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