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AMPK beta subunits: more than just a scaffold in the formation of AMPK complex
Author(s) -
Sanz Pascual,
Rubio Teresa,
GarciaGimeno Maria Adelaida
Publication year - 2013
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12364
Subject(s) - ampk , protein kinase a , phosphorylation , chemistry , amp activated protein kinase , microbiology and biotechnology , protein subunit , gamma subunit , anabolism , scaffold protein , signal transduction , biochemistry , biology , gene
AMP ‐activated protein kinase ( AMPK ) is a sensor of energy status composed of a catalytic subunit ( AMPK α), a scaffolding subunit ( AMPK β) and a regulatory subunit involved in nucleotide binding ( AMPK γ). 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. The study of the regulation of the activity of the AMPK complex has been traditionally focused on modifications of AMPK α and AMPK γ 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 β subunits are also critical players in AMPK function, because they can regulate the phosphorylation status and activity of the AMPK complex. AMPK β1‐ and AMPK β2‐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. This selective behavior opens the possibility to design specific drugs that activate AMPK complexes containing specific β‐isoforms.