Abstract
The actin cytoskeleton of eukaryotic cells is a dynamic, fibrous network that is regulated by the concerted action of actin-binding proteins (ABPs). In particular, rapid polarization of cells in response to internal and external stimuli is fundamental to cell migration and invasion. Various isoforms of ABPs in different tissues equip cells with variable degrees of migratory and adhesive capacities. In addition, regulation of ABPs by posttranslational modifications (PTM) is pivotal to the rapid responsiveness of cells. In this context, phosphorylation of ABPs and its functional consequences have been studied extensively. However, the study of reduction/oxidation (redox) modifications of oxidation-sensitive cysteine and methionine residues of actin, ABPs, adhesion molecules, and signaling proteins regulating actin cytoskeletal dynamics has only recently emerged as a field. The relevance of such protein oxidations to cellular physiology and pathophysiology has remained largely elusive. Importantly, studying protein oxidation spatiotemporally can provide novel insights into localized redox regulation of cellular functions. In this review, we focus on the redox regulation of the actin cytoskeleton, its challenges, and recently developed tools to study its physiological and pathophysiological consequences.
Highlights
Actin Cytoskeleton and actin-binding proteins (ABPs)The actin cytoskeleton is important for maintaining the shape and structure of eukaryotic cells, as well as for such essential processes as cell migration, cell polarity, intracellular or extracellular trafficking, cell-cell interactions, and cell division
In addition to the known enhanced activity of LPL resulting from phosphorylation on Ser5 (Shinomiya et al, 2007; Wabnitz et al, 2007, 2010b), Balta et al showed that LPL is regulated by thiol oxidation at Cys101 and Cys42 residues, which could be reverted by thioredoxin 1 (Balta et al, 2019)
Signaling molecules are regulated by thiol modifications, thereby influencing actin cytoskeletal reorganization
Summary
The actin cytoskeleton is important for maintaining the shape and structure of eukaryotic cells, as well as for such essential processes as cell migration, cell polarity, intracellular or extracellular trafficking, cell-cell interactions, and cell division. These processes are regulated by ABPs through the supply of globular actin (G-actin) for polymerization, nucleation of new filaments, depolymerization and severing, capping, branching, and formation of actin bundles [reviewed in Samstag et al (2003)]. Actin-bundling proteins such as plastins form F-actin into parallel or antiparallel arrays. We highlight the importance of redox regulation of ABPs and exemplify emerging tools to study this regulation in the future
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