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Proteasomal degradation induced by DPP9-mediated processing competes with mitochondrial protein import

  • Finger, Yannik Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
  • Habich, Markus Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
  • Gerlich, Sarah Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
  • Urbanczyk, Sophia Division of Molecular Immunology Department of Internal Medicine III Nikolaus‐Fiebiger‐Center University of Erlangen‐Nürnberg Erlangen Germany
  • Logt, Erik Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
  • Koch, Julian Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
  • Schu, Laura Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
  • Lapacz, Kim Jasmin Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
  • Ali, Muna Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
  • Petrungaro, Carmelina Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
  • Salscheider, Silja Lucia Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
  • Pichlo, Christian Institute of Biochemistry University of Cologne Cologne Germany
  • Baumann, Ulrich Institute of Biochemistry University of Cologne Cologne Germany
  • Mielenz, Dirk Division of Molecular Immunology Department of Internal Medicine III Nikolaus‐Fiebiger‐Center University of Erlangen‐Nürnberg Erlangen Germany
  • Dengjel, Jörn Department of Biology University of Fribourg Fribourg Switzerland
  • Brachvogel, Bent Department of Pediatrics and Adolescent Medicine Experimental Neonatology Faculty of Medicine University of Cologne Cologne Germany - Center for Biochemistry Faculty of Medicine University of Cologne Cologne Germany
  • Hofmann, Kay Institute of Genetics University of Cologne Cologne Germany
  • Riemer, Jan Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany - Cologne Excellence Cluster on Cellular Stress Responses in Aging‐Associated Diseases (CECAD) University of Cologne Cologne Germany
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    20.08.2020
Published in:
  • The EMBO Journal. - 2020, vol. 39, no. 19, p. e103889
English Plasticity of the proteome is critical to adapt to varying conditions. Control of mitochondrial protein import contributes to this plasticity. Here, we identified a pathway that regulates mitochondrial protein import by regulated N-terminal processing. We demonstrate that dipeptidyl peptidases 8/9 (DPP8/9) mediate the N-terminal processing of adenylate kinase 2 (AK2) en route to mitochondria. We show that AK2 is a substrate of the mitochondrial disulfide relay, thus lacking an N-terminal mitochondrial targeting sequence and undergoing comparatively slow import. DPP9- mediated processing of AK2 induces its rapid proteasomal degradation and prevents cytosolic accumulation of enzymatically active AK2. Besides AK2, we identify more than 100 mitochondrial proteins with putative DPP8/9 recognition sites and demonstrate that DPP8/9 influence the cellular levels of a number of these proteins. Collectively, we provide in this study a conceptual framework on how regulated cytosolic processing controls levels of mitochondrial proteins as well as their dual localization to mitochondria and other compartments.
Faculty
Faculté des sciences et de médecine
Department
Département de Biologie
Language
  • English
Classification
Biology
License
License undefined
Identifiers
Persistent URL
https://folia.unifr.ch/unifr/documents/308905
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