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Title: Ubiquitin-dependent and -independent mitochondrial protein quality controls: implications in ageing and neurodegenerative diseases.
Authors: Germain, Doris
Abstract: The ubiquitin-independent protein quality control of matrix proteins of the mitochondrion is well characterized and until recently the mitochondrion was considered a ‘ubiquitination-free’ organelle. However, a number of studies now indicate multiple roles of the ubiquitin–proteasome pathway in the regulation and maintenance of mitochondrial integrity. Of particular interest to this review is the finding of a mitochondrial ubiquitin-dependent protein quality control and that this pathway may share similarity to the ndoplasmic eticulum- ssociated egradation (ERAD) pathway that acts to eliminate misfolded proteins from the lumen of the endoplasmic reticulum. The potential cross-talk between the ubiquitin-dependent and -independent protein quality controls and their implications in ageing and neurodegenerative diseases, notably in Parkinson's disease, are discussed.
Subjects: NEURODEGENERATION; AGING; ENDOPLASMIC reticulum; UBIQUITIN; MITOCHONDRIA
Publication: Molecular Microbiology, 2008, Vol 70, Issue 6, p1334
ISSN: 0950-382X
Publication type: Academic Journal
DOI: 10.1111/j.1365-2958.2008.06502.x

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Ubiquitin-dependent and -independent mitochondrial protein quality controls: implications in ageing and neurodegenerative diseases.