Insights into the regulation of mitochondrial functions by protein kinase A-mediated phosphorylation

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  • Shiori Akabane
    Rikkyo University Department of Life Science, , Nishi-Ikebukuro 3-34-1, Toshima-ku, Tokyo 171-8501, Japan
  • Toshihiko Oka
    Rikkyo University Department of Life Science, , Nishi-Ikebukuro 3-34-1, Toshima-ku, Tokyo 171-8501, Japan

書誌事項

公開日
2023-09-29
資源種別
journal article
権利情報
  • https://academic.oup.com/pages/standard-publication-reuse-rights
DOI
  • 10.1093/jb/mvad075
公開者
Oxford University Press (OUP)

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説明

<jats:title>Abstract</jats:title> <jats:p>Cyclic AMP (cAMP)—protein kinase A (PKA) signaling is a highly conserved pathway in eukaryotes and plays a central role in cell signaling cascades in response to environmental changes. Elevated cAMP levels promote the activation of PKA, which phosphorylates various downstream proteins. Many cytosolic and nuclear proteins, such as metabolic enzymes and transcriptional factors, have been identified as substrates for PKA, suggesting that PKA-mediated regulation occurs predominantly in the cytosol. Mitochondrial proteins are also phosphorylated by PKA, and PKA-mediated phosphorylation of mitochondrial proteins is considered to control a variety of mitochondrial functions, including oxidative phosphorylation, protein import, morphology and quality control. In this review, we outline PKA mitochondrial substrates and summarize the regulation of mitochondrial functions through PKA-mediated phosphorylation.</jats:p>

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