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Review
. 2013 Feb;25(1):30-8.
doi: 10.1016/j.ceb.2012.10.009. Epub 2012 Nov 27.

Post-translational modification and regulation of actin

Jonathan R Terman  1 , Anna Kashina
Affiliations
Review

Post-translational modification and regulation of actin

Jonathan R Terman et al. Curr Opin Cell Biol. 2013 Feb.

Abstract

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.

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Figures

Figure 1
Figure 1. Structural model of the actin subunits and their fit within the filament structure and intersubunit interactions
Front and back view of the same actin subunit is shown in each left and right panel, respectively. The key functional areas are indicated. Structure shown is based on alpha cardiac actin, PDB identifier 2A42.
Figure 2
Figure 2
Chemistries of the major actin modifications.
Figure 3
Figure 3. Structural model of the actin molecule (front and back view) with individually mapped sites for several major post-translational modifications
Residues found to undergo modifications are highlighted in yellow in each set of panels. Selected modification sites with defined effects are indicated by arrows in the corresponding panels. Structure shown is based on alpha cardiac actin, PDB identifier 2A42.
See this image and copyright information in PMC

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