Protein Quality Control Degradation in the Nucleus

Charisma Enam, Yifat Geffen, Tommer Ravid, Richard G. Gardner

Research output: Contribution to journalReview articlepeer-review

47 Scopus citations


Nuclear proteins participate in diverse cellular processes, many of which are essential for cell survival and viability. To maintain optimal nuclear physiology, the cell employs the ubiquitin-proteasome system to eliminate damaged and misfolded proteins in the nucleus that could otherwise harm the cell. In this review, we highlight the current knowledge about the major ubiquitin-protein ligases involved in protein quality control degradation (PQCD) in the nucleus and how they orchestrate their functions to eliminate misfolded proteins in different nuclear subcompartments. Many human disorders are causally linked to protein misfolding in the nucleus, hence we discuss major concepts that still need to be clarified to better understand the basis of the nuclear misfolded proteins' toxic effects. Additionally, we touch upon potential strategies for manipulating nuclear PQCD pathways to ameliorate diseases associated with protein misfolding and aggregation in the nucleus.

Original languageAmerican English
Pages (from-to)725-749
Number of pages25
JournalAnnual Review of Biochemistry
StatePublished - 20 Jun 2018

Bibliographical note

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© 2018 by Annual Reviews. All rights reserved.


  • chaperones
  • nucleus
  • protein quality control
  • proteinopathies
  • proteostasis
  • ubiquitin-protein ligases


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