Cellular maintenance of nuclear protein homeostasis.
Open accessAbstract
The accumulation and aggregation of misfolded proteins is the primary hallmark for more than 45 human degenerative diseases. These devastating disorders include Alzheimer's, Parkinson's, Huntington's, and amyotrophic lateral sclerosis. Over 15 degenerative diseases are associated with the aggregation of misfolded proteins specifically in the nucleus of cells. However, how the cell safeguards the nucleus from misfolded proteins is not entirely clear. In this review, we discuss what is currently known about the cellular mechanisms that maintain protein homeostasis in the nucleus and protect the nucleus from misfolded protein accumulation and aggregation. In particular, we focus on the chaperones found to localize to the nucleus during stress, the ubiquitin-proteasome components enriched in the nucleus, the signaling systems that might be present in the nucleus to coordinate folding and degradation, and the sites of misfolded protein deposition associated with the nucleus.
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The 26S proteasome degrades polyubiquitinated proteins and plays an important role in many cellular processes, such as proteostasis and transcriptional control.
“Also, the 26S proteasome has the capacity to degrade polyubiquitinated proteins and plays an important role in many cellular processes, such as proteostasis and transcriptional control (Durairaj and Kaiser, 2014; Gallagher et al., 2014).”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Gallagher et al., 2014
The “Nuclear PQC – ubiquitin-protein ligases” section describes the ubiquitin-proteasome system as a principal means of destroying misfolded proteins, supporting its role in proteostasis. Our copy does not specifically identify the 26S proteasome as degrading polyubiquitinated proteins or establish a role for it in transcriptional control; the “Nuclear PQC – signaling pathways” discussion of transcription does not make that link. (LLM, conf=0.85)
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Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy
Kitajima, Y., Suzuki, N., Yoshioka, K., Izumi, R., Tateyama, M., Tashiro, Y., Takahashi, R., Aoki, M., & Ono, Y. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00859 · Cited by 14 · see citing works
“Also, the 26S proteasome has the capacity to degrade polyubiquitinated proteins and plays an important role in many cellular processes, such as proteostasis and transcriptional control (Durairaj and Kaiser, 2014; Gallagher et al., 2014).”
Background
- Authors
- Gallagher, P. S., Oeser, M. L., Abraham, A.-C., Kaganovich, D., & Gardner, R. G.
- Affiliations
- University of Washington (US)
- Hebrew University of Jerusalem (IL)
- Corresponding author
- Gardner, Richard G.
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2013-12-05
- Volume
- 71
- Issue
- 10
- Pages
- 1865-1879
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC3999211
- OpenAlex
- W2155665855
- Cited by
- 22
- References
- 166
- Citations by year
- 2023: 1 · 2022: 5 · 2020: 1 · 2019: 1 · 2017: 7 · 2015: 4 · 2014: 3
- FWCI
- 0.22
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cellular and Molecular Life Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- ePrints Soton (University of Southampton) (submittedVersion)
- Funders
- National Institute on Aging (R01AG031136)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- ubiquitin-proteasome system, protein degradation, neurodegenerative diseases, protein folding, protein quality control
- MeSH terms
- Cell Nucleus, Homeostasis, Humans, Nuclear Proteins, Signal Transduction, Molecular Chaperones, Ubiquitin, Ubiquitin-Protein Ligases, Proteasome Endopeptidase Complex, Sumoylation
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