Journal article
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Proteasomal degradation induced by DPP9-mediated processing competes with mitochondrial protein import
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Finger, Yannik
Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
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Habich, Markus
Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
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Gerlich, Sarah
Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
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Urbanczyk, Sophia
Division of Molecular Immunology Department of Internal Medicine III Nikolaus‐Fiebiger‐Center University of Erlangen‐Nürnberg Erlangen Germany
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Logt, Erik
Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
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Koch, Julian
Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
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Schu, Laura
Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
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Lapacz, Kim Jasmin
Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
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Ali, Muna
Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
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Petrungaro, Carmelina
Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
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Salscheider, Silja Lucia
Institute of Biochemistry Redox Biochemistry University of Cologne Cologne Germany
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Pichlo, Christian
Institute of Biochemistry University of Cologne Cologne Germany
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Baumann, Ulrich
Institute of Biochemistry University of Cologne Cologne Germany
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Mielenz, Dirk
Division of Molecular Immunology Department of Internal Medicine III Nikolaus‐Fiebiger‐Center University of Erlangen‐Nürnberg Erlangen Germany
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Dengjel, Jörn
Department of Biology University of Fribourg Fribourg Switzerland
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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
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Hofmann, Kay
Institute of Genetics University of Cologne Cologne Germany
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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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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.
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Faculty
- Faculté des sciences et de médecine
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Department
- Département de Biologie
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Language
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Classification
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Biological sciences
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License
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License undefined
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Identifiers
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Persistent URL
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https://folia.unifr.ch/unifr/documents/308905
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