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AMPK-dependent activation of the Cyclin Y/CDK16 complex controls autophagy

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  • Marc Dohmen

    (Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University
    Center for Translational & Clinical Research Aachen (CTC-A), Medical School, RWTH Aachen University)

  • Sarah Krieg

    (Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University)

  • Georgios Agalaridis

    (Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University
    Miltenyi Biotec GmbH)

  • Xiaoqing Zhu

    (CARIM School for Cardiovascular Diseases, Maastricht University)

  • Saifeldin N. Shehata

    (Nestlé Research)

  • Elisabeth Pfeiffenberger

    (Division of Molecular Pathophysiology, Biocenter, Innsbruck Medical University)

  • Jan Amelang

    (Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University)

  • Mareike Bütepage

    (Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University)

  • Elena Buerova

    (Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University)

  • Carolina M. Pfaff

    (Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University
    AstraZeneca GmbH)

  • Dipanjan Chanda

    (CARIM School for Cardiovascular Diseases, Maastricht University)

  • Stephan Geley

    (Division of Molecular Pathophysiology, Biocenter, Innsbruck Medical University)

  • Christian Preisinger

    (Proteomics Facility, Interdisciplinary Center for Clinical Research (IZKF) Aachen, Medical School, RWTH Aachen University)

  • Kei Sakamoto

    (Nestlé Research
    Novo Nordisk Foundation Center for Basic Metabolic Research, University of Copenhagen)

  • Bernhard Lüscher

    (Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University)

  • Dietbert Neumann

    (CARIM School for Cardiovascular Diseases, Maastricht University
    Department of Pathology, University Medical Center Maastricht)

  • Jörg Vervoorts

    (Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University)

Abstract

The AMP-activated protein kinase (AMPK) is a master sensor of the cellular energy status that is crucial for the adaptive response to limited energy availability. AMPK is implicated in the regulation of many cellular processes, including autophagy. However, the precise mechanisms by which AMPK controls these processes and the identities of relevant substrates are not fully understood. Using protein microarrays, we identify Cyclin Y as an AMPK substrate that is phosphorylated at Serine 326 (S326) both in vitro and in cells. Phosphorylation of Cyclin Y at S326 promotes its interaction with the Cyclin-dependent kinase 16 (CDK16), thereby stimulating its catalytic activity. When expressed in cells, Cyclin Y/CDK16 is sufficient to promote autophagy. Moreover, Cyclin Y/CDK16 is necessary for efficient AMPK-dependent activation of autophagy. This functional interaction is mediated by AMPK phosphorylating S326 of Cyclin Y. Collectively, we define Cyclin Y/CDK16 as downstream effector of AMPK for inducing autophagy.

Suggested Citation

  • Marc Dohmen & Sarah Krieg & Georgios Agalaridis & Xiaoqing Zhu & Saifeldin N. Shehata & Elisabeth Pfeiffenberger & Jan Amelang & Mareike Bütepage & Elena Buerova & Carolina M. Pfaff & Dipanjan Chanda , 2020. "AMPK-dependent activation of the Cyclin Y/CDK16 complex controls autophagy," Nature Communications, Nature, vol. 11(1), pages 1-18, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14812-0
    DOI: 10.1038/s41467-020-14812-0
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    Cited by:

    1. Yao Li & Yun Yan & Bo Gong & Qianwen Zheng & Haiyan Zhou & Jiarui Sun & Mingpeng Li & Zhao Wang & Yaohui Li & Yunjing Wan & Weixi Chen & Shiqian Qi & Xianming Mo & Anming Meng & Bo Xiang & Jing Chen, 2024. "A Huluwa phosphorylation switch regulates embryonic axis induction," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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