Involvement of mitochondrial dynamics in the segregation of mitochondrial matrix proteins during stationary phase mitophagy

Hagai Abeliovich (), Mostafa Zarei, Kristoffer T. G. Rigbolt, Richard J. Youle and Joern Dengjel
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Hagai Abeliovich: The Institute for Biochemistry, Food Science, and Nutrition, Robert H. Smith Faculty of Agriculture, Food and Environment, Hebrew University of Jerusalem
Mostafa Zarei: FRIAS, Albertstr. 19, and BIOSS, Centre for Biological Signaling Studies, University of Freiburg
Kristoffer T. G. Rigbolt: FRIAS, Albertstr. 19, and BIOSS, Centre for Biological Signaling Studies, University of Freiburg
Richard J. Youle: Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, Porter Neuroscience Research Center Building 35
Joern Dengjel: FRIAS, Albertstr. 19, and BIOSS, Centre for Biological Signaling Studies, University of Freiburg

Nature Communications, 2013, vol. 4, issue 1, 1-11

Abstract: Abstract Mitophagy, the autophagic degradation of mitochondria, is an important housekeeping function in eukaryotic cells, and defects in mitophagy correlate with ageing phenomena and with several neurodegenerative disorders. A central mechanistic question regarding mitophagy is whether mitochondria are consumed en masse, or whether an active process segregates defective molecules from functional ones within the mitochondrial network, thus allowing a more efficient culling mechanism. Here we combine a proteomic study with a molecular genetics and cell biology approach to determine whether such a segregation process occurs in yeast mitochondria. We find that different mitochondrial matrix proteins undergo mitophagic degradation at distinctly different rates, supporting the active segregation hypothesis. These differential degradation rates depend on mitochondrial dynamics, suggesting a mechanism coupling weak physical segregation with mitochondrial dynamics to achieve a distillation-like effect. In agreement, the rates of mitophagic degradation strongly correlate with the degree of physical segregation of specific matrix proteins.

Date: 2013
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DOI: 10.1038/ncomms3789

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