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Phosphorylation of mitochondrial matrix proteins regulates their selective mitophagic degradation

  • Kolitsida, Panagiota Institute of Biochemistry, Food Science and Nutrition, Hebrew University of Jerusalem, Israel
  • Zhou, Jianwen Department of Biology, University of Fribourg, Switzerland
  • Rackiewicz, Michal Department of Biology, University of Fribourg, Switzerland
  • Nolic, Vladimir Institute of Biochemistry, Food Science and Nutrition, Hebrew University of Jerusalem, Israel
  • Dengjel, Jörn Department of Biology, University of Fribourg, Switzerland - Department of Dermatology, Medical Center–University of Freiburg, Germany - Freiburg Institute for Advanced Studies, University of Freiburg, Germany
  • Abeliovich, Hagai Institute of Biochemistry, Food Science and Nutrition, Hebrew University of Jerusalem, Israel - Freiburg Institute for Advanced Studies, University of Freiburg, Germany
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    08.10.2019
Published in:
  • Proceedings of the National Academy of Sciences. - 2019, vol. 116, no. 41, p. 20517–20527
English Mitophagy is an important quality-control mechanism in eukaryotic cells, and defects in mitophagy correlate with aging phenomena and neurodegenerative disorders. It is known that different mitochondrial matrix proteins undergo mitophagy with very different rates but, to date, the mechanism underlying this selectivity at the individual protein level has remained obscure. We now present evidence indicating that protein phosphorylation within the mitochondrial matrix plays a mechanistic role in regulating selective mitophagic degradation in yeast via involvement of the Aup1 mitochondrial protein phosphatase, as well as 2 known matrix-localized protein kinases, Pkp1 and Pkp2. By focusing on a specific matrix phosphoprotein reporter, we also demonstrate that phospho-mimetic and nonphosphorylatable point mutations at known phosphosites in the reporter increased or decreased its tendency to undergo mitophagy. Finally, we show that phosphorylation of the reporter protein is dynamically regulated during mitophagy in an Aup1-dependent manner. Our results indicate that structural determinants on a mitochondrial matrix protein can govern its mitophagic fate, and that protein phosphorylation regulates these determinants.
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/308303
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