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

Marc Dohmen, Sarah Krieg, Georgios Agalaridis, Xiaoqing Zhu, Saifeldin N. Shehata, Elisabeth Pfeiffenberger, Jan Amelang, Mareike Bütepage, Elena Buerova, Carolina M. Pfaff, Dipanjan Chanda, Stephan Geley, Christian Preisinger, Kei Sakamoto, Bernhard Lüscher (), Dietbert Neumann () and Jörg Vervoorts ()
Additional contact information
Marc Dohmen: Institute of Biochemistry and Molecular Biology, 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
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
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
Bernhard Lüscher: Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University
Dietbert Neumann: CARIM School for Cardiovascular Diseases, Maastricht University
Jörg Vervoorts: Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University

Nature Communications, 2020, vol. 11, issue 1, 1-18

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-14812-0

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