| Autor: |
Braakman, Ineke, Nolden, Mark, Kisters-Woike, Brigitte, Langer, Thomas, Graef, Martin |
| Zdroj: |
Chaperones; 2006, p119-147, 29p |
| Abstrakt: |
The quality control of proteins within mitochondria is ensured by conserved and ubiquitous ATP-dependent molecular chaperones and proteases, present in various subcompartments of the organelle. Hsp70 chaperones drive protein import and facilitate folding of newly imported preproteins, but are also required for proteolysis of misfolded polypeptides by ATP-dependent proteases. Energy dependent proteases in mitochondria include Lon and Clp proteases in the matrix space and two AAA proteases in the inner membrane, all of them compartmental proteases of the AAA+ family with chaperone-like properties. Studies in yeast identify essential regulatory roles of these proteases for mitochondrial genome integrity, gene expression, the assembly of the respiratory chain, and mitochondrial morphology. An impaired proteolytic system in mitochondria has been identified as a cause for neurodegeneration in human. The present review summarizes the current understanding of the protein quality system in mitochondria and discusses the molecular action of protein machineries involved. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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