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Journal of Biochemistry Advance Access originally published online on August 7, 2009
Journal of Biochemistry 2009 146(4):455-461; doi:10.1093/jb/mvp122
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© The Authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved

JB Minireviews-Quality Control of the Cellular Protein Systems

Protein Quality Control in Mitochondria

Takashi Tatsuta*

Institute for Genetics, University of Cologne, Cologne, Germany

*To whom correspondence should be addressed. Tel: +49-221-470-4856, Fax: +49-221-470-6748, E-mail: T.Tatsuta{at}uni-koeln.de

Received May 22, 2009; Accepted June 8, 2009


  Abstract

Mitochondria are crucial for both life and death of eukaryotic cells. Compromised mitochondrial integrity has severe cellular consequences and is linked to senescence and neurodegenerative disorders in humans. To maintain the functionality of proteins in mitochondria, quality-control mechanisms including signal transduction pathways counteracting mitochondrial stress have evolved. A network of molecular chaperones and proteases monitors protein integrity and prevents accumulation of damaged proteins. In this review, the current knowledge of elaborate defence strategies within mitochondria is summarized.

Key Words: mitochondria, ATP-dependent proteases, chaperones, mitochondrial unfolded protein response, protein aggregation

Abbreviations: QC, quality control; ROS, reactive oxygen species; IM, inner membrane; OM, outer membrane; IMS, intermembrane space; TOM, translocator of outer membrane; TIM, translocator of inner membrane; NH, n-terminal helices; CH, c-terminal helices; ERAD, endoplasmic reticulum associated degradation; SCF complex, Skp1-Cullin-F-box complex; UPR, unfolded protein response; OTC, ornitine transcarbamylase; MURE, mitochondrial unfolded protein response element


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