Quality control of cytoplasmic proteins inside the nucleus
A complex network of molecular chaperones and proteolytic machinery safeguards the proteins which comprise the proteome, from the time they are synthesized on ribosomes to their destruction via proteolysis. Impaired protein quality control results in the accumulation of aberrant proteins, which may...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2022-01-01
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| Series: | Computational and Structural Biotechnology Journal |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2001037022003671 |
| _version_ | 1828087974407962624 |
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| author | Lion Borgert Swadha Mishra Fabian den Brave |
| author_facet | Lion Borgert Swadha Mishra Fabian den Brave |
| author_sort | Lion Borgert |
| collection | DOAJ |
| description | A complex network of molecular chaperones and proteolytic machinery safeguards the proteins which comprise the proteome, from the time they are synthesized on ribosomes to their destruction via proteolysis. Impaired protein quality control results in the accumulation of aberrant proteins, which may undergo unwanted spurious interactions with other proteins, thereby interfering with a broad range of cellular functions. To protect the cellular environment, such proteins are degraded or sequestered into inclusions in different subcellular compartments. Recent findings demonstrate that aberrant or mistargeted proteins from different cytoplasmic compartments are removed from their environment by transporting them into the nucleus. These proteins are degraded by the nuclear ubiquitin–proteasome system or sequestered into intra-nuclear inclusions. Here, we discuss the emerging role of the nucleus as a cellular quality compartment based on recent findings in the yeast Saccharomyces cerevisiae. We describe the current knowledge on cytoplasmic substrates of nuclear protein quality control, the mechanism of nuclear import of such proteins, as well as possible advantages and risks of nuclear sequestration of aberrant proteins. |
| first_indexed | 2024-04-11T05:19:35Z |
| format | Article |
| id | doaj.art-7aeb2908854d499bbf65936f59cbd10d |
| institution | Directory Open Access Journal |
| issn | 2001-0370 |
| language | English |
| last_indexed | 2024-04-11T05:19:35Z |
| publishDate | 2022-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Computational and Structural Biotechnology Journal |
| spelling | doaj.art-7aeb2908854d499bbf65936f59cbd10d2022-12-24T04:54:00ZengElsevierComputational and Structural Biotechnology Journal2001-03702022-01-012046184625Quality control of cytoplasmic proteins inside the nucleusLion Borgert0Swadha Mishra1Fabian den Brave2Institute of Biochemistry and Molecular Biology, Faculty of Medicine, University of Bonn, 53115 Bonn, GermanyInstitute of Biochemistry and Molecular Biology, Faculty of Medicine, University of Bonn, 53115 Bonn, GermanyCorresponding author.; Institute of Biochemistry and Molecular Biology, Faculty of Medicine, University of Bonn, 53115 Bonn, GermanyA complex network of molecular chaperones and proteolytic machinery safeguards the proteins which comprise the proteome, from the time they are synthesized on ribosomes to their destruction via proteolysis. Impaired protein quality control results in the accumulation of aberrant proteins, which may undergo unwanted spurious interactions with other proteins, thereby interfering with a broad range of cellular functions. To protect the cellular environment, such proteins are degraded or sequestered into inclusions in different subcellular compartments. Recent findings demonstrate that aberrant or mistargeted proteins from different cytoplasmic compartments are removed from their environment by transporting them into the nucleus. These proteins are degraded by the nuclear ubiquitin–proteasome system or sequestered into intra-nuclear inclusions. Here, we discuss the emerging role of the nucleus as a cellular quality compartment based on recent findings in the yeast Saccharomyces cerevisiae. We describe the current knowledge on cytoplasmic substrates of nuclear protein quality control, the mechanism of nuclear import of such proteins, as well as possible advantages and risks of nuclear sequestration of aberrant proteins.http://www.sciencedirect.com/science/article/pii/S2001037022003671Protein quality controlUbiquitin-proteasome systemChaperonesNucleusMitochondriaProtein aggregation |
| spellingShingle | Lion Borgert Swadha Mishra Fabian den Brave Quality control of cytoplasmic proteins inside the nucleus Computational and Structural Biotechnology Journal Protein quality control Ubiquitin-proteasome system Chaperones Nucleus Mitochondria Protein aggregation |
| title | Quality control of cytoplasmic proteins inside the nucleus |
| title_full | Quality control of cytoplasmic proteins inside the nucleus |
| title_fullStr | Quality control of cytoplasmic proteins inside the nucleus |
| title_full_unstemmed | Quality control of cytoplasmic proteins inside the nucleus |
| title_short | Quality control of cytoplasmic proteins inside the nucleus |
| title_sort | quality control of cytoplasmic proteins inside the nucleus |
| topic | Protein quality control Ubiquitin-proteasome system Chaperones Nucleus Mitochondria Protein aggregation |
| url | http://www.sciencedirect.com/science/article/pii/S2001037022003671 |
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