Protein Quality Control in the Nucleus
In their natural environment, cells are regularly exposed to various stress conditions that may lead to protein misfolding, but also in the absence of stress, misfolded proteins occur as the result of mutations or failures during protein synthesis. Since such partially denatured proteins are prone t...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2014-07-01
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| Series: | Biomolecules |
| Subjects: | |
| Online Access: | http://www.mdpi.com/2218-273X/4/3/646 |
| _version_ | 1818615186480693248 |
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| author | Sofie V. Nielsen Esben G. Poulsen Caio A. Rebula Rasmus Hartmann-Petersen |
| author_facet | Sofie V. Nielsen Esben G. Poulsen Caio A. Rebula Rasmus Hartmann-Petersen |
| author_sort | Sofie V. Nielsen |
| collection | DOAJ |
| description | In their natural environment, cells are regularly exposed to various stress conditions that may lead to protein misfolding, but also in the absence of stress, misfolded proteins occur as the result of mutations or failures during protein synthesis. Since such partially denatured proteins are prone to aggregate, cells have evolved several elaborate quality control systems to deal with these potentially toxic proteins. First, various molecular chaperones will seize the misfolded protein and either attempt to refold the protein or target it for degradation via the ubiquitin-proteasome system. The degradation of misfolded proteins is clearly compartmentalized, so unique degradation pathways exist for misfolded proteins depending on whether their subcellular localization is ER/secretory, mitochondrial, cytosolic or nuclear. Recent studies, mainly in yeast, have shown that the nucleus appears to be particularly active in protein quality control. Thus, specific ubiquitin-protein ligases located in the nucleus, target not only misfolded nuclear proteins, but also various misfolded cytosolic proteins which are transported to the nucleus prior to their degradation. In comparison, much less is known about these mechanisms in mammalian cells. Here we highlight recent advances in our understanding of nuclear protein quality control, in particular regarding substrate recognition and proteasomal degradation. |
| first_indexed | 2024-12-16T16:29:54Z |
| format | Article |
| id | doaj.art-d4e1404010114cd1991199d8df098471 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-12-16T16:29:54Z |
| publishDate | 2014-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-d4e1404010114cd1991199d8df0984712022-12-21T22:24:38ZengMDPI AGBiomolecules2218-273X2014-07-014364666110.3390/biom4030646biom4030646Protein Quality Control in the NucleusSofie V. Nielsen0Esben G. Poulsen1Caio A. Rebula2Rasmus Hartmann-Petersen3Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200 Copenhagen N, DenmarkDepartment of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200 Copenhagen N, DenmarkDepartment of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200 Copenhagen N, DenmarkDepartment of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200 Copenhagen N, DenmarkIn their natural environment, cells are regularly exposed to various stress conditions that may lead to protein misfolding, but also in the absence of stress, misfolded proteins occur as the result of mutations or failures during protein synthesis. Since such partially denatured proteins are prone to aggregate, cells have evolved several elaborate quality control systems to deal with these potentially toxic proteins. First, various molecular chaperones will seize the misfolded protein and either attempt to refold the protein or target it for degradation via the ubiquitin-proteasome system. The degradation of misfolded proteins is clearly compartmentalized, so unique degradation pathways exist for misfolded proteins depending on whether their subcellular localization is ER/secretory, mitochondrial, cytosolic or nuclear. Recent studies, mainly in yeast, have shown that the nucleus appears to be particularly active in protein quality control. Thus, specific ubiquitin-protein ligases located in the nucleus, target not only misfolded nuclear proteins, but also various misfolded cytosolic proteins which are transported to the nucleus prior to their degradation. In comparison, much less is known about these mechanisms in mammalian cells. Here we highlight recent advances in our understanding of nuclear protein quality control, in particular regarding substrate recognition and proteasomal degradation.http://www.mdpi.com/2218-273X/4/3/646ubiquitindegradationchaperoneproteasomemisfoldingstressSUMO |
| spellingShingle | Sofie V. Nielsen Esben G. Poulsen Caio A. Rebula Rasmus Hartmann-Petersen Protein Quality Control in the Nucleus Biomolecules ubiquitin degradation chaperone proteasome misfolding stress SUMO |
| title | Protein Quality Control in the Nucleus |
| title_full | Protein Quality Control in the Nucleus |
| title_fullStr | Protein Quality Control in the Nucleus |
| title_full_unstemmed | Protein Quality Control in the Nucleus |
| title_short | Protein Quality Control in the Nucleus |
| title_sort | protein quality control in the nucleus |
| topic | ubiquitin degradation chaperone proteasome misfolding stress SUMO |
| url | http://www.mdpi.com/2218-273X/4/3/646 |
| work_keys_str_mv | AT sofievnielsen proteinqualitycontrolinthenucleus AT esbengpoulsen proteinqualitycontrolinthenucleus AT caioarebula proteinqualitycontrolinthenucleus AT rasmushartmannpetersen proteinqualitycontrolinthenucleus |