Expanding PML's functional repertoire through post-translational mechanisms

Front Biosci (Landmark Ed). 2009 Jan 1;14:2293-306. doi: 10.2741/3380.

Abstract

Post-translational modifications, such as acetylation and ubiquitination, can greatly expand the functionality of a particular protein. The promyelocytic leukemia (PML) protein is a functionally promiscuous protein with proposed roles in many cellular processes. Its cellular headquarters are the macromolecular structures termed PML nuclear bodies. Post-translational modification of PML is emerging as a defining feature of this protein that regulates its physiological consequences. This review will highlight the expansion of our knowledge about the post-translational modifications of PML.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Humans
  • Nuclear Proteins / metabolism
  • Nuclear Proteins / physiology*
  • Phosphorylation
  • Promyelocytic Leukemia Protein
  • Protein Processing, Post-Translational*
  • Receptors, Retinoic Acid / metabolism
  • Retinoic Acid Receptor alpha
  • Small Ubiquitin-Related Modifier Proteins / metabolism
  • Transcription Factors / metabolism
  • Transcription Factors / physiology*
  • Tumor Suppressor Proteins / metabolism
  • Tumor Suppressor Proteins / physiology*

Substances

  • Nuclear Proteins
  • Promyelocytic Leukemia Protein
  • RARA protein, human
  • Receptors, Retinoic Acid
  • Retinoic Acid Receptor alpha
  • Small Ubiquitin-Related Modifier Proteins
  • Transcription Factors
  • Tumor Suppressor Proteins
  • PML protein, human