AMP-activated protein kinase: also regulated by ADP?

D. Grahame Hardie, David Carling, Steven J. Gamblin

    Research output: Contribution to journalReview article

    119 Citations (Scopus)

    Abstract

    AMPK is a ubiquitous sensor of cellular energy status in eukaryotic cells. It is activated by stresses causing ATP depletion and, once activated, maintains energy homeostasis by phosphorylating targets that activate catabolism and inhibit energy-consuming processes. Evidence derived from non-mammalian orthologs suggests that its ancestral role was in the response to starvation for a carbon source. We review recent findings showing that AMPK is activated by ADP as well as AMP, and discuss the mechanism by which binding of these nucleotides prevent its dephosphorylation and inactivation. We also discuss the role of the carbohydrate-binding module on the beta subunit and the mechanisms by which it is activated by drugs and xenobiotics such as metformin and resveratrol.

    Original languageEnglish
    Pages (from-to)470-477
    Number of pages8
    JournalTrends in Biochemical Sciences
    Volume36
    Issue number9
    DOIs
    Publication statusPublished - Sep 2011

    Keywords

    • SACCHAROMYCES-CEREVISIAE
    • UPSTREAM KINASE
    • SKELETAL-MUSCLE
    • RAT-LIVER
    • 3-HYDROXY-3-METHYLGLUTARYL COENZYME
    • ENCEPHALITOZOON-CUNICULI
    • REDUCTASE KINASE
    • STRUCTURAL BASIS
    • KEY REGULATOR
    • YEAST SNF1

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