Actin turnover ensures uniform tension distribution during cytokinetic actomyosin ring contraction

Cheffings, Thomas H.; Burroughs, Nigel John; Balasubramanian, Mohan K.

doi:10.1091/mbc.e18-08-0511

Cited by 16 publications

(30 citation statements)

References 29 publications

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“…Arp2/3 complex was purified from calf thymus by WASp(VCA) affinity chromatography 60 . WASP fragment construct GST-human WASp pWA was purified by Glutathione-Sepharose affinity chromatography 29 .…”

Section: Lim Protein Expression In Fission Yeastmentioning

confidence: 99%

Evolutionarily diverse LIM domain-containing proteins bind stressed actin filaments through a conserved mechanism

Winkelman

Anderson

Suarez

et al. 2020

Preprint

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The actin cytoskeleton assembles into diverse load-bearing networks including stress fibers, muscle sarcomeres, and the cytokinetic ring to both generate and sense mechanical forces. The LIM (Lin11, Isl-1 & Mec-3) domain family is functionally diverse, but most members can associate with the actin cytoskeleton with apparent force-sensitivity. Zyxin rapidly localizes via its LIM domains to failing stress fibers in cells, known as strain sites, to initiate stress fiber repair and maintain mechanical homeostasis. The mechanism by which these LIM domains associate with stress fiber strain sites is not known. Additionally, it is unknown how widespread strain sensing is within the LIM protein family. We observe that many, but not all, LIM domains from functionally diverse proteins localize to spontaneous or induced stress fiber strain sites in mammalian cells. Additionally, the LIM domain region from the fission yeast protein paxillin like 1 (Pxl1) also localizes to stress fiber strain sites in mammalian cells, suggesting that the strain sensing mechanism is ancient and highly conserved. Sequence analysis and mutagenesis of the LIM domain region of zyxin indicate a requirement of tandem LIM domains, which contribute additively, for sensing stress fiber strain sites. In vitro, purified LIM domains from mammalian zyxin and fission yeast Pxl1 bind to mechanically stressed F-actin networks but do not associate with relaxed actin filaments. We propose that tandem LIM domains recognize an F-actin conformation that is rare in the relaxed state but is enriched in the presence of mechanical stress. Cells are subject to a wide range of omnipresent mechanical stimuli, which play essential physiological roles. Epithelial tissue stretch modulates cell proliferation 1,2 , blood pressure regulates the contractility of endothelial cells within blood vessels 3,4 , and muscle contraction shapes connective tissue remodeling 5 . Such mechanotransduction pathways allow for the integration of mechanical cues with the biochemical and genetic circuitry of the cell. While much progress has been made to elucidate the importance of mechanical stimuli in cell physiology, the underlying force-sensing mechanisms and organizational logic of many mechanotransduction pathways are unknown.To respond to mechanical cues and dynamically modulate cell mechanics, the actin cytoskeleton exploits force-sensitive biochemistry to construct actin filament (F-actin)-based network assemblies. Focal adhesions, the adhesive organelles between cells and their external matrix, can change in composition and size under varied mechanical load 6 . At the molecular scale, these focal adhesion changes arise primarily from force-dependent modulation of constituent proteins 6-8 . The force-dependent association of the focal adhesion proteins, vinculin and talin, to actin filaments is sensitive to filament polarity 9,10 , providing a mechanism to guide local cytoskeletal architecture under load. Protrusive forces at the leading edge of migrating cells are generated by actin po...

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Section: Lim Protein Expression In Fission Yeastmentioning

confidence: 99%

Evolutionarily diverse LIM domain-containing proteins bind stressed actin filaments through a conserved mechanism

Winkelman

Anderson

Suarez

et al. 2020

Preprint

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“…1A, B). We never observed abnormal ring structures such as detachment from the cell wall (Arasada and Pollard, 2014;Laplante et al, 2015;Cheffings et al, 2019), therefore we consider Rlc1-tdTomato constriction to reflect furrow ingression. Thirty percent of these fully-formed contractile rings slid along the membrane of cps1-191 cells at 36°C, as reported (Arasada and Pollard, 2014;Cortés et al, 2015).…”

Section: Resultsmentioning

confidence: 84%

Microtubule Nucleation Promoters Mto1 and Mto2 Regulate Cytokinesis in Fission Yeast

Dundon

Pollard

2019

Preprint

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Dundon and Pollard show that compromising the Mto1 or Mto2 regulators of the fission yeast γtubulin complex reduces or eliminates astral microtubules, exaggerates the effects of a non-lethal D277N substitution in β-glucan synthase 1 (Cps1/Bgs1) on the rate of cytokinetic furrow formation, and increases Rho-GTP at the cleavage site. AbstractMicrotubules of the mitotic spindle direct cytokinesis in metazoans but this has not been documented in fungi. We report evidence that astral microtubules help coordinate cytokinetic furrow formation in fission yeast. The temperature-sensitive cps1-191 strain (Liu et al., 1999) with a D277N substitution in β-glucan synthase 1 (Cps1/Bgs1) was reported to arrest with an unconstricted contractile ring. We discovered that rings in cps1-191 cells do constrict slowly and that an S338N mutation in the mto2 gene is required with the bgs1 D277N mutation to reproduce the cps1-191 phenotype. Complexes of Mto2 and Mto1 with γ-tubulin regulate microtubule assembly. Deletion of Mto1 along with the bgs1 D277N mutation also gives the cps1-191 phenotype, which is not observed in mto2 S338N or mto1Δ cells expressing bgs1 + . Both mto2 S338N and mto1Δ cells nucleate fewer astral microtubules than normal and have higher levels of Rho1-GTP at the division site than wild-type cells. We report multiple conditions that sensitize mto1Δ and mto2 S338N cells to furrow ingression phenotypes. (159 words)

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“…Los protoplastos son células a las que se les elimina la pared celular mediante digestión enzimática (Stachowiak et al 2014). Los sistemas semi-in vitro conocidos como "fantasmas celulares" utilizan protoplastos permeabilizados para eliminar el material citoplásmico (Mangione & Gould 2019 (Cheffings et al 2019).…”

Section: Constricción Del Anillounclassified

“…Dejando de lado la vía de la miosina estudiamos si el bloqueo del CAR podía venir dado por alteraciones en los procesos de remodelación de actina. Se sabe que tanto la polimerización como la despolimerización de los filamentos de actina son actividades necesarias para la integridad y constricción del CAR (Cheffings et al 2016(Cheffings et al , 2019Rincon & Paoletti 2016). La formina Cdc12 nuclea y elonga los filamentos de actina (Chang et al 1997;Kovar et al 2003), mientras que la cofilina Adf1 participa en la remodelación seccionando estos (Nakano & Mabuchi 2006).…”

Section: Relación De La Actina Con El Retraso Causado Por El Estrés Eunclassified

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Regulación de la citoquinesis por Rgf1 y la ruta de integridad

González¹

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Actin turnover ensures uniform tension distribution during cytokinetic actomyosin ring contraction

Cited by 16 publications

References 29 publications

Evolutionarily diverse LIM domain-containing proteins bind stressed actin filaments through a conserved mechanism

Evolutionarily diverse LIM domain-containing proteins bind stressed actin filaments through a conserved mechanism

Microtubule Nucleation Promoters Mto1 and Mto2 Regulate Cytokinesis in Fission Yeast

Regulación de la citoquinesis por Rgf1 y la ruta de integridad

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