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    AMPK signaling to acetyl-CoA carboxylase is required for fasting- and cold-induced appetite but not thermogenesis

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    Author
    Galic, S; Loh, K; Murray-Segal, L; Steinberg, GR; Andrews, ZB; Kemp, BE
    Date
    2018-01-30
    Source Title
    eLife
    Publisher
    ELIFE SCIENCES PUBLICATIONS LTD
    University of Melbourne Author/s
    Kemp, Bruce; Steinberg, Gregory; Galic, Sandra; Andrews, Zane
    Affiliation
    Medicine and Radiology
    University General
    Metadata
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    Document Type
    Journal Article
    Citations
    Galic, S., Loh, K., Murray-Segal, L., Steinberg, G. R., Andrews, Z. B. & Kemp, B. E. (2018). AMPK signaling to acetyl-CoA carboxylase is required for fasting- and cold-induced appetite but not thermogenesis. ELIFE, 7, https://doi.org/10.7554/eLife.32656.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/253360
    DOI
    10.7554/eLife.32656
    Abstract
    AMP-activated protein kinase (AMPK) is a known regulator of whole-body energy homeostasis, but the downstream AMPK substrates mediating these effects are not entirely clear. AMPK inhibits fatty acid synthesis and promotes fatty acid oxidation by phosphorylation of acetyl-CoA carboxylase (ACC) 1 at Ser79 and ACC2 at Ser212. Using mice with Ser79Ala/Ser212Ala knock-in mutations (ACC DKI) we find that inhibition of ACC phosphorylation leads to reduced appetite in response to fasting or cold exposure. At sub-thermoneutral temperatures, ACC DKI mice maintain normal energy expenditure and thermogenesis, but fail to increase appetite and lose weight. We demonstrate that the ACC DKI phenotype can be mimicked in wild type mice using a ghrelin receptor antagonist and that ACC DKI mice have impaired orexigenic responses to ghrelin, indicating ACC DKI mice have a ghrelin signaling defect. These data suggest that therapeutic strategies aimed at inhibiting ACC phosphorylation may suppress appetite following metabolic stress.

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