Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia


Langer,  T.
Department Langer - Mitochondrial Proteostasis, Max Planck Institute for Biology of Ageing, Max Planck Society;

External Resource
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available

Rugarli, E. I., & Langer, T. (2006). Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia. Trends Mol Med, 12(6), 262-9. doi:10.1016/j.molmed.2006.04.002.

Cite as: https://hdl.handle.net/21.11116/0000-000B-7287-C
Hereditary spastic paraplegia (HSP) is a genetically heterogeneous neurodegenerative disorder that is characterized by progressive and cell-specific axonal degeneration. An autosomal recessive form of the disease is caused by mutations in paraplegin, which is a conserved subunit of the ubiquitous and ATP-dependent m-AAA protease in mitochondria. The m-AAA protease carries out protein quality control in the inner membrane of the mitochondria, suggesting a pathogenic role of misfolded proteins in HSP. A recent study demonstrates that the m-AAA protease regulates ribosome assembly and translation within mitochondria by controlling proteolytic maturation of a ribosomal subunit. Here, we will discuss implications of the dual role of the m-AAA protease in protein activation and degradation for mitochondrial dysfunction and axonal degeneration.