Post-translational modification and regulation of actin

Curr Opin Cell Biol. 2013 Feb;25(1):30-8. doi: 10.1016/ Epub 2012 Nov 27.


Many of the best-studied actin regulatory proteins use non-covalent means to modulate the properties of actin. Yet, actin is also susceptible to covalent modifications of its amino acids. Recent work is increasingly revealing that actin processing and its covalent modifications regulate important cellular events. In addition, numerous pathogens express enzymes that specifically use actin as a substrate to regulate their hosts' cells. Actin post-translational alterations have been linked to different normal and disease processes and the effects associated with metabolic and environmental stressors. Herein, we highlight specific co-translational and post-translational modifications of actin and discuss the current understanding of the role that these modifications play in regulating actin.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • ADP Ribose Transferases / metabolism
  • Acetylation
  • Actins / chemistry*
  • Actins / metabolism*
  • Animals
  • Glycosylation
  • Humans
  • Methylation
  • Oxidation-Reduction
  • Protein Processing, Post-Translational*
  • Sumoylation
  • Ubiquitination


  • Actins
  • ADP Ribose Transferases