Actin filaments—A target for redox regulation

Carlos Wilson, Jonathan R. Terman, Christian González-Billault, Giasuddin Ahmed

Research output: Contribution to journalReview article

30 Scopus citations

Abstract

Actin and its ability to polymerize into dynamic filaments is critical for the form and function of cells throughout the body. While multiple proteins have been characterized as affecting actin dynamics through noncovalent means, actin and its protein regulators are also susceptible to covalent modifications of their amino acid residues. In this regard, oxidation-reduction (Redox) intermediates have emerged as key modulators of the actin cytoskeleton with multiple different effects on cellular form and function. Here, we review work implicating Redox intermediates in post-translationally altering actin and discuss what is known regarding how these alterations affect the properties of actin. We also focus on two of the best characterized enzymatic sources of these Redox intermediates—the NADPH oxidase NOX and the flavoprotein monooxygenase MICAL—and detail how they have both been identified as altering actin, but share little similarity and employ different means to regulate actin dynamics. Finally, we discuss the role of these enzymes and redox signaling in regulating the actin cytoskeleton in vivo and highlight their importance for neuronal form and function in health and disease.

Original languageEnglish (US)
Pages (from-to)577-595
Number of pages19
JournalCytoskeleton
Volume73
Issue number10
DOIs
StatePublished - Oct 1 2016

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Keywords

  • actin
  • MICAL
  • NADPH oxidase
  • post-translational modification
  • redox

ASJC Scopus subject areas

  • Structural Biology
  • Cell Biology

Cite this

Wilson, C., Terman, J. R., González-Billault, C., & Ahmed, G. (2016). Actin filaments—A target for redox regulation. Cytoskeleton, 73(10), 577-595. https://doi.org/10.1002/cm.21315