Actin filaments-A target for redox regulation.
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. © 2016 Wiley Periodicals, Inc.
Department of Biology, Faculty of Sciences, Universidad De Chile, Las Palmeras 3425, Santiago, 7800024, Chile.|Center for Geroscience, Brain Health and Metabolism, Santiago, Chile.
Carlos
C
Wilson
Department of Neuroscience, The University of Texas Southwestern Medical Center, Dallas, Texas, 75390. chrgonza@uchile.cl.|Department of Pharmacology, The University of Texas Southwestern Medical Center, Dallas, Texas, 75390. chrgonza@uchile.cl.
Jonathan R
JR
Terman
Department of Biology, Faculty of Sciences, Universidad De Chile, Las Palmeras 3425, Santiago, 7800024, Chile. jonathan.terman@utsouthwestern.edu.|Center for Geroscience, Brain Health and Metabolism, Santiago, Chile. jonathan.terman@utsouthwestern.edu.|The Buck Institute for Research on Aging, Novato, California 94945. jonathan.terman@utsouthwestern.edu.
Christian
C
González-Billault
Department of Neuroscience, The University of Texas Southwestern Medical Center, Dallas, Texas, 75390.|Department of Pharmacology, The University of Texas Southwestern Medical Center, Dallas, Texas, 75390.
Giasuddin
G
Ahmed
D008841:Actin Cytoskeleton / Q000378:metabolism*; D000199:Actins / Q000378:metabolism*; D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism*; D000818:Animals; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D006801:Humans; D060588:LIM Domain Proteins / Q000378:metabolism*; D008840:Microfilament Proteins; D006899:Mixed Function Oxygenases; D019255:NADPH Oxidases / Q000378:metabolism*; D010084:Oxidation-Reduction; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology*; D000096985:Calponins
D000199:Actins; D048868:Adaptor Proteins, Signal Transducing; D003598:Cytoskeletal Proteins; D060588:LIM Domain Proteins; D008840:Microfilament Proteins; D006899:Mixed Function Oxygenases; D019255:NADPH Oxidases; C455272:MICAL1 protein, human; D000096985:Calponins
MICAL; NADPH oxidase; actin; post-translational modification; redox