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Curr Opin Cell Biol. 2011 Aug;23(4):476-82. doi: 10.1016/j.ceb.2011.05.007. Epub 2011 Jun 24.

Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation.

Author information

1
Center for Biomedical Engineering and Technology and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA. mkarbowski@umaryland.edu

Abstract

Mitochondrial outer membrane proteins have been found to be ubiquitinated and degraded by the proteasome. This process shares at least one component of the ERAD pathway of ER membrane protein degradation, the AAA ATPase cdc48/p97/VCP, thought to extract integral membrane proteins from the lipid bilayer and chaperone them to the proteasome. Proteasomal degradation of the outer mitochondrial membrane (OMM) protein Mcl1 regulates apoptosis whereas Parkin-mediated ubiquitination and degradation of Mitofusins can inhibit mitochondrial fusion and promote mitophagy. The breadth of OMM ubiquitin/proteasome substrates and the physiological relevance of their turnover are only beginning to be understood.

PMID:
21705204
PMCID:
PMC3155757
DOI:
10.1016/j.ceb.2011.05.007
[Indexed for MEDLINE]
Free PMC Article

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