Control of mitochondrial biogenesis and function by the ubiquitin–proteasome system
Mitochondria are pivotal organelles in eukaryotic cells. The complex proteome of mitochondria comprises proteins that are encoded by nuclear and mitochondrial genomes. The biogenesis of mitochondrial proteins requires their transport in an unfolded state with a high risk of misfolding. The mislocali...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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The Royal Society
2017-01-01
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| Series: | Open Biology |
| Subjects: | |
| Online Access: | https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.170007 |
| _version_ | 1818967039505596416 |
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| author | Piotr Bragoszewski Michal Turek Agnieszka Chacinska |
| author_facet | Piotr Bragoszewski Michal Turek Agnieszka Chacinska |
| author_sort | Piotr Bragoszewski |
| collection | DOAJ |
| description | Mitochondria are pivotal organelles in eukaryotic cells. The complex proteome of mitochondria comprises proteins that are encoded by nuclear and mitochondrial genomes. The biogenesis of mitochondrial proteins requires their transport in an unfolded state with a high risk of misfolding. The mislocalization of mitochondrial proteins is deleterious to the cell. The electron transport chain in mitochondria is a source of reactive oxygen species that damage proteins. Mitochondrial dysfunction is linked to many pathological conditions and, together with the loss of cellular protein homeostasis (proteostasis), are hallmarks of ageing and ageing-related degeneration diseases. The pathogenesis of neurodegenerative disorders, such as Alzheimer's disease and Parkinson's disease, has been associated with mitochondrial and proteostasis failure. Thus, mitochondrial proteins require sophisticated surveillance mechanisms. Although mitochondria form a proteasome-exclusive compartment, multiple lines of evidence indicate a crucial role for the cytosolic ubiquitin–proteasome system (UPS) in the quality control of mitochondrial proteins. The proteasome affects mitochondrial proteins at stages of their biogenesis and maturity. The effects of the UPS go beyond the removal of damaged proteins and include the adjustment of mitochondrial proteome composition, the regulation of organelle dynamics and the protection of cellular homeostasis against mitochondrial failure. In turn, mitochondrial activity and mitochondrial dysfunction adjust the activity of the UPS, with implications at the cellular level. |
| first_indexed | 2024-12-20T13:42:27Z |
| format | Article |
| id | doaj.art-4e968b4b3fa2466e818de0a0e231390b |
| institution | Directory Open Access Journal |
| issn | 2046-2441 |
| language | English |
| last_indexed | 2024-12-20T13:42:27Z |
| publishDate | 2017-01-01 |
| publisher | The Royal Society |
| record_format | Article |
| series | Open Biology |
| spelling | doaj.art-4e968b4b3fa2466e818de0a0e231390b2022-12-21T19:38:47ZengThe Royal SocietyOpen Biology2046-24412017-01-017410.1098/rsob.170007170007Control of mitochondrial biogenesis and function by the ubiquitin–proteasome systemPiotr BragoszewskiMichal TurekAgnieszka ChacinskaMitochondria are pivotal organelles in eukaryotic cells. The complex proteome of mitochondria comprises proteins that are encoded by nuclear and mitochondrial genomes. The biogenesis of mitochondrial proteins requires their transport in an unfolded state with a high risk of misfolding. The mislocalization of mitochondrial proteins is deleterious to the cell. The electron transport chain in mitochondria is a source of reactive oxygen species that damage proteins. Mitochondrial dysfunction is linked to many pathological conditions and, together with the loss of cellular protein homeostasis (proteostasis), are hallmarks of ageing and ageing-related degeneration diseases. The pathogenesis of neurodegenerative disorders, such as Alzheimer's disease and Parkinson's disease, has been associated with mitochondrial and proteostasis failure. Thus, mitochondrial proteins require sophisticated surveillance mechanisms. Although mitochondria form a proteasome-exclusive compartment, multiple lines of evidence indicate a crucial role for the cytosolic ubiquitin–proteasome system (UPS) in the quality control of mitochondrial proteins. The proteasome affects mitochondrial proteins at stages of their biogenesis and maturity. The effects of the UPS go beyond the removal of damaged proteins and include the adjustment of mitochondrial proteome composition, the regulation of organelle dynamics and the protection of cellular homeostasis against mitochondrial failure. In turn, mitochondrial activity and mitochondrial dysfunction adjust the activity of the UPS, with implications at the cellular level.https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.170007mitochondriaproteasomeubiquitinubiquitin–proteasome systemproteostasisprotein biogenesis |
| spellingShingle | Piotr Bragoszewski Michal Turek Agnieszka Chacinska Control of mitochondrial biogenesis and function by the ubiquitin–proteasome system Open Biology mitochondria proteasome ubiquitin ubiquitin–proteasome system proteostasis protein biogenesis |
| title | Control of mitochondrial biogenesis and function by the ubiquitin–proteasome system |
| title_full | Control of mitochondrial biogenesis and function by the ubiquitin–proteasome system |
| title_fullStr | Control of mitochondrial biogenesis and function by the ubiquitin–proteasome system |
| title_full_unstemmed | Control of mitochondrial biogenesis and function by the ubiquitin–proteasome system |
| title_short | Control of mitochondrial biogenesis and function by the ubiquitin–proteasome system |
| title_sort | control of mitochondrial biogenesis and function by the ubiquitin proteasome system |
| topic | mitochondria proteasome ubiquitin ubiquitin–proteasome system proteostasis protein biogenesis |
| url | https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.170007 |
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