Architecture Dependence of Actin Filament Network Disassembly

Gressin, Laurène; Guillotin, Audrey; Guérin, Christophe; Blanchoin, Laurent; Michelot, Alphée

doi:10.1016/j.cub.2015.04.011

Cited by 107 publications

(129 citation statements)

References 52 publications

(78 reference statements)

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“…Previous results show that WDR1 can bind to Cofilin-actin and induces F-actin structural changes to accelerate Cofilin severing F-actin activity (9). In addition, another report shows that WDR1 might simply compete with Cofilin and dissociate redundant Cofilin from F-actin to accelerate severing activity (44).…”

Section: Discussionmentioning

confidence: 99%

“…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).…”

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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%

mentioning

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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“…For example, barbed-end boundaries may be more readily identified than pointed-end ones. Alternatively, this behavior could arise if severing occurred preferentially at the pointed-end side of the cluster, as reported (32,33). A third possible explanation would be a mechanism in which cofilin clusters grew asymmetrically and more rapidly in the pointed-end direction (8), such that clusters extended to the filament pointed end.…”

Section: Asymmetries In Boundary Polaritymentioning

confidence: 91%

The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments

Huehn

Cao

Elam

et al. 2018

Journal of Biological Chemistry

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Cofilin/ADF proteins are actin-remodeling proteins, essential for actin disassembly in various cellular processes, including cell division, intracellular transport, and motility. Cofilins bind actin filaments cooperatively and sever them preferentially at boundaries between bare and cofilin-decorated (cofilactin) segments. The cooperative binding to actin has been proposed to originate from conformational changes that propagate allosterically from clusters of bound cofilin to bare actin segments. Estimates of the lengths over which these cooperative conformational changes propagate vary dramatically, ranging from 2 to >100 subunits. Here, we present a general, structure-based method for detecting from cryo-EM micrographs small variations in filament geometry (i.e. twist) with single subunit precision. How these variations correlate with regulatory protein occupancy reveals how far allosteric, conformational changes propagate along filaments. We used this method to determine the effects of cofilin on the actin filament twist. Our results indicate that cofilin-induced changes in filament twist propagate only 1-2 subunits from the boundary into the bare actin segment, independently of the boundary polarity (i.e. irrespective of whether or not the bare actin segment flanks the pointed or barbed end side of the boundary) and the pyrene fluorophore labeling of actin. These observations indicate that the filament twist changes abruptly at boundaries between bare and cofilin-decorated segments, thereby constraining mechanistic models of cooperative actin filament interactions and severing by cofilin. The methods presented here extend the capability of cryo-EM to analyze biologically relevant deviations from helical symmetry in actin as well as other classes of linear polymers.

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“…The latter effect is responsible for enhanced growth of individual filament barbed ends, which supports motility. Recently, other factors such as Aip1 (also known as DAB2IP), coronin proteins, twinfilin proteins and cyclase-associated proteins (CAP, Srv2 in yeast) have been reported to further enhance filament disassembly in synergy with ADF and cofilin proteins (Gressin et al, 2015;Johnston et al, 2015;Kueh et al, 2008;Mikati et al, 2015;Nadkarni and Brieher, 2014). These effects, however, do not appear to involve barbed-end capping by these proteins, in contrast with what has been previously suggested (Okada et al, 2002).…”

Section: Indirect Regulation Of Barbed-end Growth By Adf and Cofilin mentioning

confidence: 98%

Regulators of actin filament barbed ends at a glance

Shekhar

Pernier

Carlier

2016

Journal of Cell Science

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Cells respond to external stimuli by rapidly remodeling their actin cytoskeleton. At the heart of this function lies the intricately controlled regulation of individual filaments. The barbed end of an actin filament is the hotspot for the majority of the biochemical reactions that control filament assembly. Assays performed in bulk solution and with single filaments have enabled characterization of a plethora of barbed-endregulating proteins. Interestingly, many of these regulators work in tandem with other proteins, which increase or decrease their affinity for the barbed end in a spatially and temporally controlled manner, often through simultaneous binding of two regulators at the barbed ends, in addition to standard mutually exclusive binding schemes. In this Cell Science at a Glance and the accompanying poster, we discuss key barbed-end-interacting proteins and the kinetic mechanisms by which they regulate actin filament assembly. We take F-actin capping protein, gelsolin, profilin and barbed-endtracking polymerases, including formins and WH2-domaincontaining proteins, as examples, and illustrate how their activity and competition for the barbed end regulate filament dynamics.

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Architecture Dependence of Actin Filament Network Disassembly

Cited by 107 publications

References 52 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

The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments

Regulators of actin filament barbed ends at a glance

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