Quality control of mitochondrial proteostasis

A decline in mitochondrial activity has been associated with aging and is a hallmark of many neurological diseases. Surveillance mechanisms acting at the molecular, organellar, and cellular level monitor mitochondrial integrity and ensure the maintenance of mitochondrial proteostasis. Here we will r...

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Bibliographic Details
Published in:	Cold Spring Harbor perspectives in biology 2011-07, Vol.3 (7), p.a007559-a007559
Main Authors:	Baker, Michael J, Tatsuta, Takashi, Langer, Thomas
Format:	Article
Language:	eng
Subjects:	Adenosine Triphosphate - metabolism Animals Cellular Senescence GTP Phosphohydrolases - metabolism GTP Phosphohydrolases - physiology Homeostasis Humans Mitochondria - metabolism Mitochondria - physiology Mitochondria - ultrastructure Mitochondrial Proteins - metabolism Mitochondrial Proteins - physiology Models, Biological Molecular Chaperones - metabolism Molecular Chaperones - physiology Peptide Hydrolases - metabolism Peptide Hydrolases - physiology Proteasome Endopeptidase Complex - metabolism Proteasome Endopeptidase Complex - physiology Protein Folding Ubiquitin - metabolism
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Summary:	A decline in mitochondrial activity has been associated with aging and is a hallmark of many neurological diseases. Surveillance mechanisms acting at the molecular, organellar, and cellular level monitor mitochondrial integrity and ensure the maintenance of mitochondrial proteostasis. Here we will review the central role of mitochondrial chaperones and proteases, the cytosolic ubiquitin-proteasome system, and the mitochondrial unfolded response in this interconnected quality control network, highlighting the dual function of some proteases in protein quality control within the organelle and for the regulation of mitochondrial fusion and mitophagy.
ISSN:	1943-0264 1943-0264