SnapShot: Actin Regulators I

Siripala, Anosha D.; Welch, Matthew D.

doi:10.1016/j.cell.2007.02.001

Cited by 21 publications

(24 citation statements)

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“…This includes the conserved role of essential components, such as AIP1 and CFL1 (Poukkula et al, 2011;Siripala and Welch, 2007), and the potent actin network retrograde flow resulting from actin assembly (Forscher and Smith, 1988). Importantly, our genetic investigations led to the identification of cytoskeleton factors, such as GMFB, TWF2 and CAP1 that genetically interact with AIP1.…”

Section: Discussionmentioning

confidence: 99%

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Actin network disassembly powersListeria monocytogenesdissemination

Talman

Chong

Chia

et al. 2013

Journal of Cell Science

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Several bacterial pathogens hijack the actin assembly machinery and display intracellular motility in the cytosol of infected cells. At the cell cortex, intracellular motility leads to bacterial dissemination through formation of plasma membrane protrusions that resolve into vacuoles in adjacent cells. Here, we uncover a crucial role for actin network disassembly in dissemination of Listeria monocytogenes. We found that defects in the disassembly machinery decreased the rate of actin tail turnover but did not affect the velocity of the bacteria in the cytosol. By contrast, defects in the disassembly machinery had a dramatic impact on bacterial dissemination. Our results suggest a model of L. monocytogenes dissemination in which the disassembly machinery, through local recycling of the actin network in protrusions, fuels continuous actin assembly at the bacterial pole and concurrently exhausts cytoskeleton components from the network distal to the bacterium, which enables membrane apposition and resolution of protrusions into vacuoles.

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Section: Discussionmentioning

confidence: 99%

“…1B). We next used the spreading assay to screen a siRNA library targeting genes encoding regulators of the actin cytoskeleton (Siripala and Welch, 2007) (supplementary material Table S1). The library harbored four independent siRNA duplexes targeting a given gene.…”

Section: Identification Of Host Factors Required For L Monocytogenesmentioning

confidence: 99%

Actin network disassembly powersListeria monocytogenesdissemination

Talman

Chong

Chia

et al. 2013

Journal of Cell Science

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“…Spatial and temporal control of these functions is achieved by an arsenal of actin-associated proteins, which regulate the nucleation, elongation, cross-linking, and disassembly of filaments (Siripala & Welch, 2007). For example, at the sites of endocytosis in yeast and mammals, more than 50 different proteins function to regulate the rapid assembly and turnover of a distinctive, architecturally complex actin network and drive endocytic vesicle internalization within 15–20 s (Boettner, Friesen, Andrews, & Lemmon, 2011; Weinberg & Drubin, 2012).…”

Section: Introductionmentioning

confidence: 99%

Single-Molecule Studies of Actin Assembly and Disassembly Factors

Smith

Gelles

Goode

2014

Methods in Enzymology

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The actin cytoskeleton is very dynamic and highly regulated by multiple associated proteins in vivo. Understanding how this system of proteins functions in the processes of actin network assembly and disassembly requires methods to dissect the mechanisms of activity of individual factors and of multiple factors acting in concert. The advent of single-filament and single-molecule fluorescence imaging methods has provided a powerful new approach to discovering actin-regulatory activities and obtaining direct, quantitative insights into the pathways of molecular interactions that regulate actin network architecture and dynamics. Here we describe techniques for acquisition and analysis of single-molecule data, applied to the novel challenges of studying the filament assembly and disassembly activities of actin-associated proteins in vitro. We discuss the advantages of single-molecule analysis in directly visualizing the order of molecular events, measuring the kinetic rates of filament binding and dissociation, and studying the coordination among multiple factors. The methods described here complement traditional biochemical approaches in elucidating actin-regulatory mechanisms in reconstituted filamentous networks.

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“…Long lists of actin-associated proteins from Rho GTPases, kinases, phosphatases, and actin-binding proteins regulate actin filament dynamics (1,3,4,(6)(7)(8). Actinbundling proteins such as α-actinin, fascin, and filamin cross-link actin filaments into bundles and play important roles in regulating membrane protrusions and cell mobility (9)(10)(11)(12)(13). Cofilin severs existing actin filaments to generate more free ends and thus plays a critical role in actin dynamics (9,10,14,15).…”

mentioning

confidence: 99%

“…Actinbundling proteins such as α-actinin, fascin, and filamin cross-link actin filaments into bundles and play important roles in regulating membrane protrusions and cell mobility (9)(10)(11)(12)(13). Cofilin severs existing actin filaments to generate more free ends and thus plays a critical role in actin dynamics (9,10,14,15). The protein epithelial protein lost in neoplasm (eplin) bundles F-actin filaments and can control G-actin nucleation by regulating the activity of the Arp2/3 actin complex (16).…”

mentioning

confidence: 99%

Human phosphatase CDC14A regulates actin organization through dephosphorylation of epithelial protein lost in neoplasm

Chen

Uddin

Hardt

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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CDC14 is an essential dual-specificity phosphatase that counteracts CDK1 activity during anaphase to promote mitotic exit in Saccharomyces cerevisiae. Surprisingly, human CDC14A is not essential for cell cycle progression. Instead, it regulates cell migration and cell adhesion. Little is known about the substrates of hCDC14A and the counteracting kinases. Here, we combine phospho-proteome profiling and proximity-dependent biotin identification to identify hCDC14A substrates. Among these targets were actin regulators, including the tumor suppressor eplin. hCDC14A counteracts EGF-induced rearrangements of actin cytoskeleton by dephosphorylating eplin at two known extracellular signal-regulated kinase sites, serine 362 and 604. hCDC14A(PD) and eplin knockout cell lines exhibited down-regulation of E-cadherin and a reduction in alpha/beta-catenin at cell-cell adhesions. Reduction in the levels of hCDC14A and eplin mRNA is frequently associated with colorectal carcinoma and is correlated with poor prognosis. We therefore propose that eplin dephosphorylation by hCDC14A reduces actin dynamics to restrict tumor malignancy

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SnapShot: Actin Regulators I

Cited by 21 publications

References 0 publications

Actin network disassembly powersListeria monocytogenesdissemination

Actin network disassembly powersListeria monocytogenesdissemination

Single-Molecule Studies of Actin Assembly and Disassembly Factors

Human phosphatase CDC14A regulates actin organization through dephosphorylation of epithelial protein lost in neoplasm

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