Ins and outs of ADF/cofilin activity and regulation

Troys, Marleen Van; Huyck, Lynn; Leyman, Shirley; Dhaese, Stien; Vandekerkhove, Joël; Ampè, Christophe

doi:10.1016/j.ejcb.2008.04.001

Cited by 284 publications

(277 citation statements)

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“…Cofilin is important for spatial and temporal regulation of F-actin dynamics in cells and its activity is tightly controlled by several mechanisms (7,41,42). However, which mechanism is the most important process for Cofilin severing activity is still unclear.…”

Section: Discussionmentioning

confidence: 99%

“…However, which mechanism is the most important process for Cofilin severing activity is still unclear. Cofilin binding and severing F-actin activity is dependent upon its phosphorylation, which is tightly regulated by the protein kinases and phosphatases in vivo, such as LIMK and SSH (15,42). In response to the stimuli, the kinases phosphorylate, whereas the phosphatases dephosphorylate Cofilin to control its interaction with actin for optimal severing activity to regulate the dynamics of actin cytoskeleton (14,44).…”

Section: Discussionmentioning

confidence: 99%

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Trp-Asp (WD) Repeat Domain 1 Is Essential for Mouse Peri-implantation Development and Regulates Cofilin Phosphorylation

Xiao

Wan

et al. 2017

Journal of Biological Chemistry

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Edited by Xiao-Fan WangTrp-Asp (WD) repeat domain 1 (WDR1) is a highly conserved actin-binding protein across all eukaryotes and is involved in numerous actin-based processes by accelerating Cofilin severing actin filament. However, the function and the mechanism of WDR1 in mammalian early development are still largely unclear. We now report that WDR1 is essential for mouse periimplantation development and regulates Cofilin phosphorylation in mouse cells. The disruption of maternal WDR1 does not obviously affect ovulation and female fertility. However, depletion of zygotic WDR1 results in embryonic lethality at the periimplantation stage. In WDR1 knock-out cells, we found that WDR1 regulates Cofilin phosphorylation. Interestingly, WDR1 is overdosed to regulate Cofilin phosphorylation in mouse cells. Furthermore, we showed that WDR1 interacts with Lim domain kinase 1 (LIMK1), a well known phosphorylation kinase of Cofilin. Altogether, our results provide new insights into the role and mechanism of WDR1 in physiological conditions.The actin cytoskeleton is a highly dynamic structure that regulates cell motility, adhesion, division, and growth and has a fundamental function in embryonic development (1-3). In physiological conditions, actin filaments are continually assembled and disassembled in response to varied cellular activities (4, 5). The dynamics of F-actin is well orchestrated by a large number of actin-binding proteins (5, 6). Actin-depolymerizing factor Cofilin plays critical roles in the modulation of actin cytoskeleton dynamics (7). In vitro, Cofilin severs actin filament at low concentrations, whereas it fully decorates actin filaments and suppresses the severing activity at high concentrations (8, 9). In addition, Cofilin severing F-actin is not explained well for how the filaments of actin cytoskeleton can be rapidly disassembled in physiological conditions (4). Thus, the function of Cofilin in actin dynamics depends not only on its relative concentration to actin, but also on other regulatory proteins in vivo. Dysfunction of these regulating proteins results in aberrant actin cytoskeleton in various cellular and developmental processes (10 -12).Cofilin directly binds with actin to function as a regulator of the actin dynamics (13). However, the phosphorylation of Cofilin at Ser-3 blocks its binding site to actin (14, 15). Thus, the activity of Cofilin is controlled by phosphorylation and dephosphorylation processes, which are regulated by cascade reactions of several protein kinases and phosphatases. Lim domain kinases (LIMKs) 4 and testis-specific protein kinases (TESKs) are responsible for the phosphorylation of Cofilin, whereas slingshot (SSH) family protein phosphatases and pyridoxal phosphatase (PDXP) catalyze the dephosphorylation reaction (16 -20). These kinases and phosphatases are also regulated by their phosphorylation or localization in cytoplasm to maintain the level of Cofilin phosphorylation in response to extracellular stimuli (21-23).The activity of Cofilin on actin disassembly is gr...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Trp-Asp (WD) Repeat Domain 1 Is Essential for Mouse Peri-implantation Development and Regulates Cofilin Phosphorylation

Xiao

Wan

et al. 2017

Journal of Biological Chemistry

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“…Cof-1 is a key regulator of cell motility by inducing F-actin depolymerization and severing (37). Phosphorylation of Cof-1 at serine 3 leads to loss of actin binding and severing activities and subsequently results in decreased cell motility (33). Actin remodeling and its impact on cell migration have an essential function in a variety of cellular processes such as cell movement, cell adhesion, and cytokinesis (38).…”

Section: Discussionmentioning

confidence: 99%

Prolyl Hydroxylase Domain (PHD) 2 Affects Cell Migration and F-actin Formation via RhoA/Rho-associated Kinase-dependent Cofilin Phosphorylation

Vogel

Wottawa

Farhat

et al. 2010

Journal of Biological Chemistry

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Cells are responding to hypoxia via prolyl-4-hydroxylase domain (PHD) enzymes, which are responsible for oxygen-dependent hydroxylation of the hypoxia-inducible factor (HIF)-1␣ subunit. To gain further insight into PHD function, we generated knockdown cell models for the PHD2 isoform, which is the main isoform regulating HIF-1␣ hydroxylation and thus stability in normoxia. Induction of a PHD2 knockdown in tetracycline-inducible HeLa PHD2 knockdown cells resulted in increased F-actin formation as detected by phalloidin staining. A similar effect could be observed in the stably transfected PHD2 knockdown cell clones 1B6 and 3B7. F-actin is at least in part responsible for shaping cell morphology as well as regulating cell migration. Cell migration was impaired significantly as a consequence of PHD2 knockdown in a scratch assay. Mechanistically, PHD2 knockdown resulted in activation of the RhoA (Ras homolog gene family member A)/Rho-associated kinase pathway with subsequent phosphorylation of cofilin. Because cofilin phosphorylation impairs its actin-severing function, this may explain the F-actin phenotype, thereby providing a functional link between PHD2-dependent signaling and cell motility.

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“…An example is the modification of the expression level of actin-depolymerization factor (ADF)/cofilin encoding genes. The ADF/cofilin family has emerged as a central regulator of actin turnover in eukaryotes including plants [Bamburg, 1999;Maciver and Hussey, 2002;Van Troys et al, 2008]. Through its AF severing and pointed enddepolymerizing activities, ADF/cofilin enhances actin cytoskeleton dynamics [Carlier et al, 1997;Blanchoin and Pollard, 1999;Pavlov et al, 2007].…”

Section: Actin Bundling Versus Depolymerization Forcesmentioning

confidence: 99%

“…Within the cells, actin filament (AF) assembly and disassembly are facilitated at spatial and temporal levels by a plethora of actin-binding proteins (ABPs), including nucleating, depolymerizing, severing, capping, F-actin stabilizing and G-actin sequestering proteins [Dos Remedios et al, 2003]. Among the repertoire of actin-binding proteins (ABPs) that regulate AF dynamics, one may cite key players such as the Arp2/3 complex and formins, which direct the initiation of new branched and unbranched filaments respectively [Pollard, 2007], as well as the actindepolymerizing factor (ADF)/cofilin family members, which increase filament turnover [Bamburg et al, 1999;Van Troys et al, 2008]. An additional level of regulation is the assembly of AFs into higher-order structures such as orthogonal networks and parallel bundles by a specialized subset of ABPs, which are able to crosslink adjacent filaments through bivalent actin-binding [Puius et al, 1998].…”

Section: Introductionmentioning

confidence: 99%

Actin bundling in plants

Thomas

Tholl

Moes

et al. 2009

Cell Motil. Cytoskeleton

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Tight regulation of plant actin cytoskeleton organization and dynamics is crucial for numerous cellular processes including cell division, expansion and intracellular trafficking. Among the various actin regulatory proteins, actin-bundling proteins trigger the formation of bundles composed of several parallel actin filaments closely packed together. Actin bundles are present in virtually all plant cells, but their biological roles have rarely been addressed directly. However, decades of research in the plant cytoskeleton field yielded a bulk of data from which an overall picture of the functions supplied by actin bundles in plant cells emerges. Although plants lack several equivalents of animal actin-bundling proteins, they do possess major bundler classes including fimbrins, villins and formins. The existence of additional players is not excluded as exemplified by the recent characterization of plant LIM proteins, which trigger the formation of actin bundles both in vitro and in vivo. This apparent functional redundancy likely reflects the need for plant cells to engineer different types of bundles that act at different sub-cellular locations and exhibit specific function-related properties. By surveying information regarding the properties of plant actin bundles and their associated bundling proteins, the present review aims at clarifying why and how plants make actin bundles. Cell Motil. Cytoskeleton 66: 940-957, 2009. '

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Ins and outs of ADF/cofilin activity and regulation

Cited by 284 publications

References 129 publications

Trp-Asp (WD) Repeat Domain 1 Is Essential for Mouse Peri-implantation Development and Regulates Cofilin Phosphorylation

Trp-Asp (WD) Repeat Domain 1 Is Essential for Mouse Peri-implantation Development and Regulates Cofilin Phosphorylation

Prolyl Hydroxylase Domain (PHD) 2 Affects Cell Migration and F-actin Formation via RhoA/Rho-associated Kinase-dependent Cofilin Phosphorylation

Actin bundling in plants

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