PML nuclear bodies: assembly and oxidative stress-sensitive sumoylation

Nucleus. 2014;5(6):499-507. doi: 10.4161/19491034.2014.970104.


PML Nuclear Bodies (NBs) have fascinated cell biologists due to their exquisitely dynamic nature and their involvement in human diseases, notably acute promyelocytic leukemia. NBs, as well as their master organizer--the PML protein--exhibit multiple connections with stress responses. Initially viewed as a tumor suppressor, PML recently re-emerged as a multifaceted protein, capable of controlling numerous aspects of cellular homeostasis. NBs recruit many functionally diverse proteins and function as stress-regulated sumoylation factories. SUMO-initiated partner retention can subsequently facilitate a variety of other post-translational modifications, as well as partner degradation. With this newly elucidated central role of stress-enhanced sumoylation, it should now be possible to build a working model for the different NB-regulated cellular activities. Moreover, pharmacological manipulation of NB formation by interferons or oxidants holds the promise of clearing many undesirable proteins for clinical management of malignant, viral or neurodegenerative diseases.

Keywords: PML; RNF4; SIM; SUMO; arsenic; degradation; interferon; nuclear bodies; oxidative stress; post-translational modifications; senescence.

Publication types

  • Review

MeSH terms

  • Basic Helix-Loop-Helix Transcription Factors / genetics
  • Cell Nucleus / metabolism
  • Cellular Senescence / genetics
  • Humans
  • Intranuclear Inclusion Bodies / genetics*
  • Nuclear Proteins / genetics*
  • Oxidative Stress / genetics*
  • Protein Processing, Post-Translational
  • Proteolysis
  • Repressor Proteins / genetics
  • SUMO-1 Protein / genetics*
  • Sumoylation / genetics
  • Transcription Factors / genetics*


  • Basic Helix-Loop-Helix Transcription Factors
  • Nuclear Proteins
  • RNF4 protein, human
  • Repressor Proteins
  • SIM1 protein, human
  • SUMO-1 Protein
  • Transcription Factors