Mitochondrial protein translocation-associated degradation

Christoph U. Mårtensson, Chantal Priesnitz, Jiyao Song, Lars Ellenrieder, Kim Nguyen Doan, Felix Boos, Alessia Floerchinger, Nicole Zufall, Silke Oeljeklaus, Bettina Warscheid and Thomas Becker ()
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Christoph U. Mårtensson: University of Freiburg
Chantal Priesnitz: University of Freiburg
Jiyao Song: University of Freiburg
Lars Ellenrieder: University of Freiburg
Kim Nguyen Doan: University of Freiburg
Felix Boos: University of Kaiserslautern
Alessia Floerchinger: University of Freiburg
Nicole Zufall: University of Freiburg
Silke Oeljeklaus: University of Freiburg
Bettina Warscheid: University of Freiburg
Thomas Becker: University of Freiburg

Nature, 2019, vol. 569, issue 7758, 679-683

Abstract: Abstract Mitochondrial biogenesis and functions depend on the import of precursor proteins via the ‘translocase of the outer membrane’ (TOM complex). Defects in protein import lead to an accumulation of mitochondrial precursor proteins that induces a range of cellular stress responses. However, constitutive quality-control mechanisms that clear trapped precursor proteins from the TOM channel under non-stress conditions have remained unknown. Here we report that in Saccharomyces cerevisiae Ubx2, which functions in endoplasmic reticulum-associated degradation, is crucial for this quality-control process. A pool of Ubx2 binds to the TOM complex to recruit the AAA ATPase Cdc48 for removal of arrested precursor proteins from the TOM channel. This mitochondrial protein translocation-associated degradation (mitoTAD) pathway continuously monitors the TOM complex under non-stress conditions to prevent clogging of the TOM channel with precursor proteins. The mitoTAD pathway ensures that mitochondria maintain their full protein-import capacity, and protects cells against proteotoxic stress induced by impaired transport of proteins into mitochondria.

Date: 2019
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DOI: 10.1038/s41586-019-1227-y

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