Mitochondrial protein quality control during biogenesis and aging Journal Article


Authors: Baker, B. M.; Haynes, C. M.
Article Title: Mitochondrial protein quality control during biogenesis and aging
Abstract: Mitochondrial dysfunction has long been associated with the aging process and the onset of numerous diseases. Regulation of the complex protein-folding environment within the organelle is essential for maintaining efficient metabolic output. Over time, dysregulation of protein homeostasis arises through stress induced by the accumulation of reactive oxygen species and mutations in the mitochondrial genome introduced during replication. To preserve organelle function during biogenesis, remodeling and stress, quality control of mitochondrial proteins must be monitored by molecular chaperones and proteases stationed in the four compartments of the organelle. Here, we review mitochondrial protein quality control with a focus on organelle biogenesis and aging. © 2011 Elsevier Ltd.
Keywords: review; nonhuman; dna replication; protein domain; neoplasm; quality control; proteasome; protein assembly; protein degradation; extracellular matrix; endoplasmic reticulum; protein processing; transcription regulation; ubiquitination; cell damage; protein transport; reactive oxygen metabolite; aging; caenorhabditis elegans; heat shock protein 70; protein folding; parkinson disease; mitochondrial protein; mitochondrion; oxidative phosphorylation; cell organelle; cytosol; biogenesis; cell stress; mitochondrial dna; presenilin; chaperone; disorders of mitochondrial functions; protein aggregation; outer membrane; reduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone); unfolded protein response; parkin; pdz protein; serine proteinase omi; electron transport; protein quality
Journal Title: Trends in Biochemical Sciences
Volume: 36
Issue: 5
ISSN: 0968-0004
Publisher: Elsevier Inc.  
Date Published: 2011-05-01
Start Page: 254
End Page: 261
Language: English
DOI: 10.1016/j.tibs.2011.01.004
PROVIDER: scopus
PUBMED: 21353780
DOI/URL:
Notes: --- - "Export Date: 23 June 2011" - "CODEN: TBSCD" - "Source: Scopus"
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MSK Authors
  1. Cole Haynes
    24 Haynes
  2. Brooke Baker
    4 Baker