Artículo de revista
Actin Filaments—A Target for Redox Regulation
Date
2016Registration in:
Cytoskeleton, October 2016 73:577–595
10.1002/cm.21315
Author
Wilson, Carlos
Terman, Jonathan R.
Ahmed, Giasuddin
Institutions
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 posttranslationally
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
formand function in health and disease.