Cited by 22Heat shock proteins researchNuclear Structure and FunctionUbiquitin and proteasome pathways

Cellular maintenance of nuclear protein homeostasis.

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Gallagher, Pamela S., Oeser, Michelle L., Abraham, Ayelet-chen, Kaganovich, Daniel, Gardner, Richard G.·2014·Cellular and Molecular Life Sciences

Abstract

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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Crossref · 10.1007/s00018-013-1530-y

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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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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
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
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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