Cellular and Molecular Life Sciences

, Volume 71, Issue 10, pp 1865–1879

Cellular maintenance of nuclear protein homeostasis

Authors

  • Pamela S. Gallagher
    • Department of PharmacologyUniversity of Washington
  • Michelle L. Oeser
    • Department of PharmacologyUniversity of Washington
    • Molecular and Cellular Biology ProgramUniversity of Washington
  • Ayelet-chen Abraham
    • Department of Cell and Developmental Biology, Alexander Silberman Institute of Life SciencesHebrew University of Jerusalem
  • Daniel Kaganovich
    • Department of Cell and Developmental Biology, Alexander Silberman Institute of Life SciencesHebrew University of Jerusalem
    • Department of PharmacologyUniversity of Washington
    • Molecular and Cellular Biology ProgramUniversity of Washington
Review

DOI: 10.1007/s00018-013-1530-y

Cite this article as:
Gallagher, P.S., Oeser, M.L., Abraham, A. et al. Cell. Mol. Life Sci. (2014) 71: 1865. doi:10.1007/s00018-013-1530-y

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.

Keywords

NucleusChaperoneUbiquitin-protein ligaseUbiquitinProteasomeUnfolded protein responseMisfolded proteinAggregationInclusionAggresomeJUNQ

Copyright information

© Springer Basel 2013