Journal
JOURNAL OF PROTEOMICS
Volume 92, Issue -, Pages 181-194Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jprot.2013.03.022
Keywords
Chaperone; Mitochondria; Oxidative stress; Peptidase; Protein quality control; Protein translocation
Categories
Funding
- European Research Council (ERC)
- European Commission Framework Programmes
- Greek Ministry of Education
- General Secretariat for Research and Technology post-doctoral fellowship
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Mitochondrial protein quality control incorporates an elaborate network of chaperones and proteases that survey the organelle for misfolded or unfolded proteins and toxic aggregates. Repair of misfolded or aggregated protein and proteolytic removal of irreversibly damaged proteins are carried out by the mitochondrial protein quality control system. Initial maturation and folding of the nuclear or mitochondrial-encoded mitochondrial proteins are mediated by processing peptidases and chaperones that interact with the protein translocation machinery. Mitochondrial proteins are subjected to cumulative oxidative damage. Thus, impairment of quality control processes may cause mitochondrial dysfunction. Aging has been associated with a marked decline in the effectiveness of mitochondrial protein quality control. Here, we present an overview of the chaperones and proteases involved in the initial folding and maturation of new, incoming precursor molecules, and the subsequent repair and removal of oxidized aggregated proteins. In addition, we highlight the link between mitochondrial protein quality control mechanisms and the aging process. (C) 2013 Elsevier B.V. All rights reserved.
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