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Actin filaments—A target for redox regulation
Author(s) -
Wilson Carlos,
Terman Jonathan R.,
GonzálezBillault Christian,
Ahmed Giasuddin
Publication year - 2016
Publication title -
cytoskeleton
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.95
H-Index - 86
eISSN - 1949-3592
pISSN - 1949-3584
DOI - 10.1002/cm.21315
Subject(s) - biology , actin binding protein , actin , microbiology and biotechnology , actin remodeling , actin cytoskeleton , mdia1 , cytoskeleton , redox , biochemistry , profilin , actin remodeling of neurons , function (biology) , cell , chemistry , organic chemistry
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.