Fine-Tuning TOM-Mitochondrial Import via Ubiquitin

Mohamed A Eldeeb; Andrew N Bayne; Jean-François Trempe; Edward A Fon

doi:10.1016/j.tcb.2020.04.007

Fine-Tuning TOM-Mitochondrial Import via Ubiquitin

Trends Cell Biol. 2020 Jun;30(6):425-427. doi: 10.1016/j.tcb.2020.04.007. Epub 2020 Apr 25.

Authors

Mohamed A Eldeeb¹, Andrew N Bayne², Jean-François Trempe², Edward A Fon³

Affiliations

¹ McGill Parkinson Program, Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada. Electronic address: Mohamed.eldeeb@mcgill.ca.
² Department of Pharmacology and Therapeutics and Centre de Recherche en Biologie Structurale, McGill University, Montreal, Quebec, Canada.
³ McGill Parkinson Program, Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada. Electronic address: ted.fon@mcgill.ca.

PMID: 32345464
DOI: 10.1016/j.tcb.2020.04.007

Abstract

Given their polyvalent functions, an inherent challenge that mitochondria face is the exposure to mitochondrial import stresses, culminating in their dysfunction. Recently, mitochondrial import of several mitochondrial substrates was shown to be regulated via a 'tug of war' between USP30 and MARCH5, two ubiquitin-related enzymes located at the TOM complex.

Keywords: MARCH5; TOM complex; USP30; mitochondrial quality control; proteasome; protein degradation; protein quality control; ubiquitin.

Publication types

Review

MeSH terms

Humans
Mitochondria / metabolism*
Mitochondrial Membranes / metabolism*
Mitochondrial Proteins / metabolism
Models, Biological
Protein Transport
Ubiquitin / metabolism*

Substances

Mitochondrial Proteins
Ubiquitin