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Journal articles on the topic 'Actomyosine – Contraction'

Author: Grafiati

Published: 25 May 2024

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1

Murrell, Michael, and Margaret L. Gardel. "Actomyosin sliding is attenuated in contractile biomimetic cortices." Molecular Biology of the Cell 25, no. 12 (2014): 1845–53. http://dx.doi.org/10.1091/mbc.e13-08-0450.

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Myosin II motors embedded within the actin cortex generate contractile forces to modulate cell shape in essential behaviors, including polarization, migration, and division. In sarcomeres, myosin II–mediated sliding of antiparallel F-actin is tightly coupled to myofibril contraction. By contrast, cortical F-actin is highly disordered in polarity, orientation, and length. How the disordered nature of the actin cortex affects actin and myosin movements and resultant contraction is unknown. Here we reconstitute a model cortex in vitro to monitor the relative movements of actin and myosin under co

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2

Slabodnick, Mark M., Sophia C. Tintori, Mangal Prakash, et al. "Zyxin contributes to coupling between cell junctions and contractile actomyosin networks during apical constriction." PLOS Genetics 19, no. 3 (2023): e1010319. http://dx.doi.org/10.1371/journal.pgen.1010319.

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One of the most common cell shape changes driving morphogenesis in diverse animals is the constriction of the apical cell surface. Apical constriction depends on contraction of an actomyosin network in the apical cell cortex, but such actomyosin networks have been shown to undergo continual, conveyor belt-like contractions before the shrinking of an apical surface begins. This finding suggests that apical constriction is not necessarily triggered by the contraction of actomyosin networks, but rather can be triggered by unidentified, temporally-regulated mechanical links between actomyosin and

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3

Wirshing, Alison C. E., and Erin J. Cram. "Myosin activity drives actomyosin bundle formation and organization in contractile cells of the Caenorhabditis elegans spermatheca." Molecular Biology of the Cell 28, no. 14 (2017): 1937–49. http://dx.doi.org/10.1091/mbc.e17-01-0029.

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Stress fibers—contractile actomyosin bundles—are important for cellular force production and adaptation to physical stress and have been well studied within the context of cell migration. However, less is known about actomyosin bundle formation and organization in vivo and in specialized contractile cells, such as smooth muscle and myoepithelial cells. The Caenorhabditis elegans spermatheca is a bag-like organ of 24 myoepithelial cells that houses the sperm and is the site of fertilization. During ovulation, spermathecal cells are stretched by oocyte entry and then coordinately contract to exp

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4

Krueger, Daniel, Theresa Quinkler, Simon Arnold Mortensen, Carsten Sachse, and Stefano De Renzis. "Cross-linker–mediated regulation of actin network organization controls tissue morphogenesis." Journal of Cell Biology 218, no. 8 (2019): 2743–61. http://dx.doi.org/10.1083/jcb.201811127.

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Contraction of cortical actomyosin networks driven by myosin activation controls cell shape changes and tissue morphogenesis during animal development. In vitro studies suggest that contractility also depends on the geometrical organization of actin filaments. Here we analyze the function of actomyosin network topology in vivo using optogenetic stimulation of myosin-II in Drosophila embryos. We show that early during cellularization, hexagonally arrayed actomyosin fibers are resilient to myosin-II activation. Actomyosin fibers then acquire a ring-like conformation and become contractile and se

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Martin, Adam C., Michael Gelbart, Rodrigo Fernandez-Gonzalez, Matthias Kaschube, and Eric F. Wieschaus. "Integration of contractile forces during tissue invagination." Journal of Cell Biology 188, no. 5 (2010): 735–49. http://dx.doi.org/10.1083/jcb.200910099.

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Contractile forces generated by the actomyosin cytoskeleton within individual cells collectively generate tissue-level force during epithelial morphogenesis. During Drosophila mesoderm invagination, pulsed actomyosin meshwork contractions and a ratchet-like stabilization of cell shape drive apical constriction. Here, we investigate how contractile forces are integrated across the tissue. Reducing adherens junction (AJ) levels or ablating actomyosin meshworks causes tissue-wide epithelial tears, which release tension that is predominantly oriented along the anterior–posterior (a-p) embryonic ax

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6

Yi, Jason, Xufeng S. Wu, Travis Crites, and John A. Hammer. "Actin retrograde flow and actomyosin II arc contraction drive receptor cluster dynamics at the immunological synapse in Jurkat T cells." Molecular Biology of the Cell 23, no. 5 (2012): 834–52. http://dx.doi.org/10.1091/mbc.e11-08-0731.

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Actin retrograde flow and actomyosin II contraction have both been implicated in the inward movement of T cell receptor (TCR) microclusters and immunological synapse formation, but no study has integrated and quantified their relative contributions. Using Jurkat T cells expressing fluorescent myosin IIA heavy chain and F-tractin—a novel reporter for F-actin—we now provide direct evidence that the distal supramolecular activation cluster (dSMAC) and peripheral supramolecular activation cluster (pSMAC) correspond to lamellipodial (LP) and lamellar (LM) actin networks, respectively, as hypothesiz

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7

Lippincott, J., K. B. Shannon, W. Shou, R. J. Deshaies, and R. Li. "The Tem1 small GTPase controls actomyosin and septin dynamics during cytokinesis." Journal of Cell Science 114, no. 7 (2001): 1379–86. http://dx.doi.org/10.1242/jcs.114.7.1379.

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Cytokinesis in budding yeast involves an actomyosin-based ring which assembles in a multistepped fashion during the cell cycle and constricts during cytokinesis. In this report, we have investigated the structural and regulatory events that occur at the onset of cytokinesis. The septins, which form an hour-glass like structure during early stages of the cell cycle, undergo dynamic rearrangements prior to cell division: the hourglass structure splits into two separate rings. The contractile ring, localized between the septin double rings, immediately undergoes contraction. Septin ring splitting

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8

Szymanski, P. T., J. D. Strauss, G. Doerman, J. DiSalvo, and R. J. Paul. "Polylysine activates smooth muscle actin-myosin interaction without LC20 phosphorylation." American Journal of Physiology-Cell Physiology 262, no. 6 (1992): C1446—C1455. http://dx.doi.org/10.1152/ajpcell.1992.262.6.c1446.

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Phosphorylation/dephosphorylation of the 20-kDa light chain of smooth muscle myosin is a major regulator of actin-myosin interaction. Phosphatase inhibitors have thus been shown to enhance contraction in smooth muscle. The activity of type II phosphatase against phosphorylated myosin light chains is inhibited by polylysine. Thus we studied the effects of polylysine (10-13 kDa) on actin-myosin interaction in permeabilized guinea pig taenia coli fibers and in bovine aortic actomyosin. Addition of polylysine (10-20 microM) to Ca-ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic aci

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9

Chew, Ting Gang, Junqi Huang, Saravanan Palani, et al. "Actin turnover maintains actin filament homeostasis during cytokinetic ring contraction." Journal of Cell Biology 216, no. 9 (2017): 2657–67. http://dx.doi.org/10.1083/jcb.201701104.

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Cytokinesis in many eukaryotes involves a tension-generating actomyosin-based contractile ring. Many components of actomyosin rings turn over during contraction, although the significance of this turnover has remained enigmatic. Here, using Schizosaccharomyces japonicus, we investigate the role of turnover of actin and myosin II in its contraction. Actomyosin ring components self-organize into ∼1-µm-spaced clusters instead of undergoing full-ring contraction in the absence of continuous actin polymerization. This effect is reversed when actin filaments are stabilized. We tested the idea that t

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10

VerPlank, Lynn, and Rong Li. "Cell Cycle-regulated Trafficking of Chs2 Controls Actomyosin Ring Stability during Cytokinesis." Molecular Biology of the Cell 16, no. 5 (2005): 2529–43. http://dx.doi.org/10.1091/mbc.e04-12-1090.

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Cytokinesis requires the coordination of many cellular complexes, particularly those involved in the constriction and reconstruction of the plasma membrane in the cleavage furrow. We have investigated the regulation and function of vesicle transport and fusion during cytokinesis in budding yeast. By using time-lapse confocal microscopy, we show that post-Golgi vesicles, as well as the exocyst, a complex required for the tethering and fusion of these vesicles, localize to the bud neck at a precise time just before spindle disassembly and actomyosin ring contraction. Using mutants affecting cycl

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Darenfed, Hassina, and Craig A. Mandato. "Wound-induced contractile ring: a model for cytokinesis." Biochemistry and Cell Biology 83, no. 6 (2005): 711–20. http://dx.doi.org/10.1139/o05-164.

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The actomyosin-based contractile ring is required for several biological processes, such as wound healing and cytokinesis of animal cells. Despite progress in defining the roles of this structure in both wound closure and cell division, we still do not fully understand how an actomyosin ring is spatially and temporally assembled, nor do we understand the molecular mechanism of its contraction. Recent results have demonstrated that microtubule-dependent local assembly of F-actin and myosin-II is present in wound closure and is similar to that in cytokinesis in animal cells. Furthermore, signall

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Horowitz, A., O. Clement-Chomienne, M. P. Walsh, T. Tao, H. Katsuyama, and K. G. Morgan. "Effects of calponin on force generation by single smooth muscle cells." American Journal of Physiology-Heart and Circulatory Physiology 270, no. 5 (1996): H1858—H1863. http://dx.doi.org/10.1152/ajpheart.1996.270.5.h1858.

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Although the actin-binding and actomyosin adenosinetriphosphatase (ATPase) inhibitory properties of calponin are well documented in vitro, its function in the smooth muscle cell has not been elucidated. To address this question, we utilized the ferret aortic smooth muscle cell, which shows a protein kinase C-dependent contraction even at pCa (-log [Ca2+]) 9.0 in the absence of a change in myosin light chain phosphorylation. Force was recorded from single, briefly permeabilized cells stimulated via a Ca(2+)-independent pathway by either phenylephrine or the epsilon isoenzyme of protein kinase C

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Hai, Chi-Ming, and Hak Rim Kim. "An expanded latch-bridge model of protein kinase C-mediated smooth muscle contraction." Journal of Applied Physiology 98, no. 4 (2005): 1356–65. http://dx.doi.org/10.1152/japplphysiol.00834.2004.

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A thin-filament-regulated latch-bridge model of smooth muscle contraction is proposed to integrate thin-filament-based inhibition of actomyosin ATPase activity with myosin phosphorylation in the regulation of smooth muscle mechanics. The model included two latch-bridge cycles, one of which was identical to the four-state model as proposed by Hai and Murphy ( Am J Physiol Cell Physiol 255: C86–C94, 1988), whereas the ultraslow cross-bridge cycle has lower cross-bridge cycling rates. The model-fitted phorbol ester induced slow contractions at constant myosin phosphorylation and predicted steeper

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Freundt, Johanna K., and Wolfgang A. Linke. "Titin as a force-generating muscle protein under regulatory control." Journal of Applied Physiology 126, no. 5 (2019): 1474–82. http://dx.doi.org/10.1152/japplphysiol.00865.2018.

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Titin has long been recognized as a mechanical protein in muscle cells that has a main function as a molecular spring in the contractile units, the sarcomeres. Recent work suggests that the titin spring contributes to muscle contraction in a more active manner than previously thought. In this review, we highlight this property, specifically the ability of the immunoglobulin-like (Ig) domains of titin to undergo unfolding-refolding transitions when isolated titin molecules or skeletal myofibrils are held at physiological force levels. Folding of titin Ig domains under force is a hitherto unappr

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15

Stephens, Newman L. "Smooth Muscle Contraction: Recent Advances." Canadian Journal of Physiology and Pharmacology 72, no. 11 (1994): 1317–19. http://dx.doi.org/10.1139/y94-189.

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Research in smooth muscle contraction has shown remarkable progress over the last 5 years. Striking advances have been made in the areas of biochemical regulation of contraction, centering on myosin light chain kinase activity, and of biophysical delineation of the contractile process at the actomyosin level by use of the newly developed motility assay. The purpose of the symposium held at Minaki, Ont., was to obtain a comprehensive reporting of the recent advances made in the area of smooth muscle contraction. Specifically, advances in the areas of biophysics of contraction, energetics, and c

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16

Staddon, Michael F., Edwin M. Munro, and Shiladitya Banerjee. "Pulsatile contractions and pattern formation in excitable actomyosin cortex." PLOS Computational Biology 18, no. 3 (2022): e1009981. http://dx.doi.org/10.1371/journal.pcbi.1009981.

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The actin cortex is an active adaptive material, embedded with complex regulatory networks that can sense, generate, and transmit mechanical forces. The cortex exhibits a wide range of dynamic behaviours, from generating pulsatory contractions and travelling waves to forming organised structures. Despite the progress in characterising the biochemical and mechanical components of the actin cortex, the emergent dynamics of this mechanochemical system is poorly understood. Here we develop a reaction-diffusion model for the RhoA signalling network, the upstream regulator for actomyosin assembly an

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17

Fernandez-Gonzalez, Rodrigo, and Jennifer A. Zallen. "Wounded cells drive rapid epidermal repair in the early Drosophila embryo." Molecular Biology of the Cell 24, no. 20 (2013): 3227–37. http://dx.doi.org/10.1091/mbc.e13-05-0228.

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Epithelial tissues are protective barriers that display a remarkable ability to repair wounds. Wound repair is often associated with an accumulation of actin and nonmuscle myosin II around the wound, forming a purse string. The role of actomyosin networks in generating mechanical force during wound repair is not well understood. Here we investigate the mechanisms of force generation during wound repair in the epidermis of early and late Drosophila embryos. We find that wound closure is faster in early embryos, where, in addition to a purse string around the wound, actomyosin networks at the me

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18

Spriet, Lawrence L., Karin Soderlund, and Eric Hultman. "Energy cost and metabolic regulation during intermittent and continuous tetanic contractions in human skeletal muscle." Canadian Journal of Physiology and Pharmacology 66, no. 1 (1988): 134–39. http://dx.doi.org/10.1139/y88-024.

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Muscle ATP turnover, glycogenolytic, and glycolytic rates were estimated to compare the energy cost and glycolytic regulation of 102.4 s of continuous and intermittent stimulation. Quadriceps femoris muscles of male subjects were stimulated at 20 Hz for one continuous contraction (n = 6) or a series of 64 contractions (1.6 s on, 1.6 s off; n = 6). Leg blood flow was occluded and muscle biopsies were obtained at rest and following 51.2 and 102.4 s of contraction time in both conditions. Isometric force production by the activated knee extensors decreased to 55% of initial contraction force with

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Pinar, Mario, Pedro M. Coll, Sergio A. Rincón, and Pilar Pérez. "Schizosaccharomyces pombe Pxl1 Is a Paxillin Homologue That Modulates Rho1 Activity and Participates in Cytokinesis." Molecular Biology of the Cell 19, no. 4 (2008): 1727–38. http://dx.doi.org/10.1091/mbc.e07-07-0718.

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Schizosaccharomyces pombe Rho GTPases regulate actin cytoskeleton organization and cell integrity. We studied the fission yeast gene SPBC4F6.12 based on its ability to suppress the thermosensitivity of cdc42-1625 mutant strain. This gene, named pxl1+, encodes a protein with three LIM domains that is similar to paxillin. Pxl1 does not interact with Cdc42 but it interacts with Rho1, and it negatively regulates this GTPase. Fission yeast Pxl1 forms a contractile ring in the cell division region and deletion of pxl1+ causes a delay in cell–cell separation, suggesting that it has a function in cyto

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20

Lehman, W., V. Hatch, M. Rosol, et al. "Troponin-Tropomyosin Control of Thin Filament Activity Revealed by Electron Microscopy and 3-D Reconstruction." Microscopy and Microanalysis 6, S2 (2000): 88–89. http://dx.doi.org/10.1017/s1431927600032931.

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Muscle contraction and the actomyosin ATPase that drives the contractile process are switched on and off by changes in sarcoplasmic free Ca2+ -concentration. In skeletal and cardiac muscles, on-off switching is mediated by the actinassociated protein tropomyosin and by the troponin complex. While the details of this mechanism are still subject to debate, it is well-accepted that tropomyosin strands move to sterically block and unblock myosin binding sites on actin, thereby controlling actomyosin ATPase and consequently contraction. It is also well known that the Ca2+- dependency of the movemen

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Månsson, Alf. "Hypothesis: Single Actomyosin Properties Account for Ensemble Behavior in Active Muscle Shortening and Isometric Contraction." International Journal of Molecular Sciences 21, no. 21 (2020): 8399. http://dx.doi.org/10.3390/ijms21218399.

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Muscle contraction results from cyclic interactions between myosin II motors and actin with two sets of proteins organized in overlapping thick and thin filaments, respectively, in a nearly crystalline lattice in a muscle sarcomere. However, a sarcomere contains a huge number of other proteins, some with important roles in muscle contraction. In particular, these include thin filament proteins, troponin and tropomyosin; thick filament proteins, myosin binding protein C; and the elastic protein, titin, that connects the thin and thick filaments. Furthermore, the order and 3D organization of the

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Zhang, Shi-Jin, Daniel C. Andersson, Marie E. Sandström, Håkan Westerblad, and Abram Katz. "Cross bridges account for only 20% of total ATP consumption during submaximal isometric contraction in mouse fast-twitch skeletal muscle." American Journal of Physiology-Cell Physiology 291, no. 1 (2006): C147—C154. http://dx.doi.org/10.1152/ajpcell.00578.2005.

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It is generally believed that cross bridges account for >50% of the total ATP consumed by skeletal muscle during contraction. We investigated the effect of N-benzyl- p-toluene sulfonamide (BTS), an inhibitor of myosin ATPase, on muscle force production and energy metabolism under near-physiological conditions (50-Hz stimulation frequency at 30°C results in 35% of maximal force). Extensor digitorum longus muscles from mice were isolated and stimulated to perform continuous isometric tetanic contractions. Metabolites of energy metabolism were analyzed with fluorometric techniques. ATP turnove

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Tamada, Masako, Tomas D. Perez, W. James Nelson, and Michael P. Sheetz. "Two distinct modes of myosin assembly and dynamics during epithelial wound closure." Journal of Cell Biology 176, no. 1 (2007): 27–33. http://dx.doi.org/10.1083/jcb.200609116.

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Actomyosin contraction powers the sealing of epithelial sheets during embryogenesis and wound closure; however, the mechanisms are poorly understood. After laser ablation wounding of Madin–Darby canine kidney cell monolayers, we observed distinct steps in wound closure from time-lapse images of myosin distribution during resealing. Immediately upon wounding, actin and myosin II regulatory light chain accumulated at two locations: (1) in a ring adjacent to the tight junction that circumscribed the wound and (2) in fibers at the base of the cell in membranes extending over the wound site. Rho-ki

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Kscheschinski, Bjoern, Mirna Kramar, and Karen Alim. "Calcium regulates cortex contraction in Physarum polycephalum." Physical Biology 21, no. 1 (2023): 016001. http://dx.doi.org/10.1088/1478-3975/ad0a9a.

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Abstract The tubular network-forming slime mold Physarum polycephalum is able to maintain long-scale contraction patterns driven by an actomyosin cortex. The resulting shuttle streaming in the network is crucial for the organism to respond to external stimuli and reorganize its body mass giving rise to complex behaviors. However, the chemical basis of the self-organized flow pattern is not fully understood. Here, we present ratiometric measurements of free intracellular calcium in simple morphologies of Physarum networks. The spatiotemporal patterns of the free calcium concentration reveal a n

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Harden, Nicholas, Michael Ricos, Kelly Yee, et al. "Drac1 and Crumbs participate in amnioserosa morphogenesis during dorsal closure in Drosophila." Journal of Cell Science 115, no. 10 (2002): 2119–29. http://dx.doi.org/10.1242/jcs.115.10.2119.

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Dorsal closure of the Drosophila embryo involves morphological changes in two epithelia, the epidermis and the amnioserosa, and is a popular system for studying the regulation of epithelial morphogenesis. We previously implicated the small GTPase Drac1 in the assembly of an actomyosin contractile apparatus, contributing to cell shape change in the epidermis during dorsal closure. We now present evidence that Drac1 and Crumbs, a determinant of epithelial polarity, are involved in setting up an actomyosin contractile apparatus that drives amnioserosa morphogenesis by inducing apical cell constri

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Webber, Sandra, and Dean Kriellaars. "Neuromuscular factors contributing to in vivo eccentric moment generation." Journal of Applied Physiology 83, no. 1 (1997): 40–45. http://dx.doi.org/10.1152/jappl.1997.83.1.40.

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Webber, Sandra, and Dean Kriellaars. Neuromuscular factors contributing to in vivo eccentric moment generation. J. Appl. Physiol. 83(1): 40–45, 1997.—Muscle series elasticity and its contribution to eccentric moment generation was examined in humans. While subjects [male, n = 30; age 26.3 ± 4.8 (SD) yr; body mass 78.8 ± 13.1 kg] performed an isometric contraction of the knee extensors at 60° of knee flexion, a quick stretch was imposed with a 12°-step displacement at 100°/s. The test was performed at 10 isometric activation levels ranging from 1.7 to 95.2% of maximal voluntary contraction (MVC

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Somara, Sita, and Khalil N. Bitar. "Phosphorylated HSP27 modulates the association of phosphorylated caldesmon with tropomyosin in colonic smooth muscle." American Journal of Physiology-Gastrointestinal and Liver Physiology 291, no. 4 (2006): G630—G639. http://dx.doi.org/10.1152/ajpgi.00350.2005.

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Thin-filament regulation of smooth muscle contraction involves phosphorylation, association, and dissociation of contractile proteins in response to agonist stimulation. Phosphorylation of caldesmon weakens its association with actin leading to actomyosin interaction and contraction. Present data from colonic smooth muscle cells indicate that acetylcholine induced a significant association of caldesmon with PKCα and sustained phosphorylation of caldesmon at ser789. Furthermore, acetylcholine induced significant and sustained increase in the association of phospho-caldesmon with heat-shock prot

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Rieu, Jean-Paul, Hélène Delanoë-Ayari, Seiji Takagi, Yoshimi Tanaka, and Toshiyuki Nakagaki. "Periodic traction in migrating large amoeba of Physarum polycephalum." Journal of The Royal Society Interface 12, no. 106 (2015): 20150099. http://dx.doi.org/10.1098/rsif.2015.0099.

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The slime mould Physarum polycephalum is a giant multinucleated cell exhibiting well-known Ca 2+ -dependent actomyosin contractions of its vein network driving the so-called cytoplasmic shuttle streaming. Its actomyosin network forms both a filamentous cortical layer and large fibrils. In order to understand the role of each structure in the locomotory activity, we performed birefringence observations and traction force microscopy on excised fragments of Physarum . After several hours, these microplasmodia adopt three main morphologies: flat motile amoeba, chain types with round contractile he

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Dasanayake, Nilushi L., and Anders E. Carlsson. "General Mechanism of Actomyosin Contraction." Biophysical Journal 102, no. 3 (2012): 349a. http://dx.doi.org/10.1016/j.bpj.2011.11.1913.

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Sutherland, Ann, and Alyssa Lesko. "Pulsed actomyosin contractions in morphogenesis." F1000Research 9 (February 25, 2020): 142. http://dx.doi.org/10.12688/f1000research.20874.1.

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Cell and tissue shape changes are the fundamental elements of morphogenesis that drive normal development of embryos into fully functional organisms. This requires a variety of cellular processes including establishment and maintenance of polarity, tissue growth and apoptosis, and cell differentiation, rearrangement, and migration. It is widely appreciated that the cytoskeletal networks play an important role in regulating many of these processes and, in particular, that pulsed actomyosin contractions are a core cellular mechanism driving cell shape changes and cell rearrangement. In this revi

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Mucha, David R., Carter L. Myers, and Richard C. Schaeffer. "Endothelial contraction and monolayer hyperpermeability are regulated by Src kinase." American Journal of Physiology-Heart and Circulatory Physiology 284, no. 3 (2003): H994—H1002. http://dx.doi.org/10.1152/ajpheart.00862.2002.

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Endothelial monolayer hyperpermeability is regulated by a myosin light chain phosphorylation (MLCP)-dependent contractile mechanism. In this study, we tested the role of Src-dependent tyrosine phosphorylation to modulate endothelial contraction and monolayer barrier function with the use of the myosin phosphatase inhibitor calyculin A (CalA) to directly elevate MLCP with the Src family tyrosine kinase inhibitor herbimycin A (HA) in bovine pulmonary artery endothelial cells (EC). CalA stimulated an increase in MLCP, Src kinase activity, an increase in the tyrosine phosphorylation of paxillin an

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Saadaoui, Mehdi, Didier Rocancourt, Julian Roussel, Francis Corson, and Jerome Gros. "A tensile ring drives tissue flows to shape the gastrulating amniote embryo." Science 367, no. 6476 (2020): 453–58. http://dx.doi.org/10.1126/science.aaw1965.

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Tissue morphogenesis is driven by local cellular deformations that are powered by contractile actomyosin networks. How localized forces are transmitted across tissues to shape them at a mesoscopic scale is still unclear. Analyzing gastrulation in entire avian embryos, we show that it is driven by the graded contraction of a large-scale supracellular actomyosin ring at the margin between the embryonic and extraembryonic territories. The propagation of these forces is enabled by a fluid-like response of the epithelial embryonic disk, which depends on cell division. A simple model of fluid motion

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Itoh, Katsuhiko, Takahiro Ebata, Hiroaki Hirata, et al. "DMPK is a New Candidate Mediator of Tumor Suppressor p53-Dependent Cell Death." Molecules 24, no. 17 (2019): 3175. http://dx.doi.org/10.3390/molecules24173175.

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Tumor suppressor p53 plays an integral role in DNA-damage induced apoptosis, a biological process that protects against tumor progression. Cell shape dramatically changes when cells undergo apoptosis, which is associated with actomyosin contraction; however, it remains entirely elusive how p53 regulates actomyosin contraction in response to DNA-damaging agents. To identify a novel p53 regulating gene encoding the modulator of myosin, we conducted DNA microarray analysis. We found that, in response to DNA-damaging agent doxorubicin, expression of myotonic dystrophy protein kinase (DMPK), which

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Mandato, Craig A., and William M. Bement. "Contraction and polymerization cooperate to assemble and close actomyosin rings around Xenopus oocyte wounds." Journal of Cell Biology 154, no. 4 (2001): 785–98. http://dx.doi.org/10.1083/jcb.200103105.

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Xenopus oocytes assemble an array of F-actin and myosin 2 around plasma membrane wounds. We analyzed this process in living oocytes using confocal time-lapse (four-dimensional) microscopy. Closure of wounds requires assembly and contraction of a classic “contractile ring” composed of F-actin and myosin 2. However, this ring works in concert with a 5–10-μm wide “zone” of localized actin and myosin 2 assembly. The zone forms before the ring and can be uncoupled from the ring by inhibition of cortical flow and contractility. However, contractility and the contractile ring are required for the sta

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Ratz, Paul H., and John E. Speich. "Evidence that actomyosin cross bridges contribute to “passive” tension in detrusor smooth muscle." American Journal of Physiology-Renal Physiology 298, no. 6 (2010): F1424—F1435. http://dx.doi.org/10.1152/ajprenal.00635.2009.

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Contraction of detrusor smooth muscle (DSM) at short muscle lengths generates a stiffness component we termed adjustable passive stiffness (APS) that is retained in tissues incubated in a Ca2+-free solution, shifts the DSM length-passive tension curve up and to the left, and is softened by muscle strain and release (strain softened). In the present study, we tested the hypothesis that APS is due to slowly cycling actomyosin cross bridges. APS and active tension produced by the stimulus, KCl, displayed similar length dependencies with identical optimum length values. The myosin II inhibitor ble

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Ali, Farah, Peter D. Paré, and Chun Y. Seow. "Models of contractile units and their assembly in smooth muscle." Canadian Journal of Physiology and Pharmacology 83, no. 10 (2005): 825–31. http://dx.doi.org/10.1139/y05-052.

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It is believed that the contractile filaments in smooth muscle are organized into arrays of contractile units (similar to the sarcomeric structure in striated muscle), and that such an organization is crucial for transforming the mechanical activities of actomyosin interaction into cell shortening and force generation. Details of the filament organization, however, are still poorly understood. Several models of contractile filament architecture are discussed here. To account for the linear relationship observed between the force generated by a smooth muscle and the muscle length at the plateau

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Ishigami, M., K. Kuroda, and S. Hatano. "Dynamic aspects of the contractile system in Physarum plasmodium. III. Cyclic contraction-relaxation of the plasmodial fragment in accordance with the generation-degeneration of cytoplasmic actomyosin fibrils." Journal of Cell Biology 105, no. 1 (1987): 381–86. http://dx.doi.org/10.1083/jcb.105.1.381.

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Plasmodial fragments of Physarum polycephalum, excised from anterior regions of a thin-spread plasmodium, contracted-relaxed cyclicly with a period of 3-5 min. The area of the fragments decreased approximately 10% during contraction. In most cases, there was little endoplasmic streaming which indicates that contractions were synchronized throughout the fragment. By both polarized light and fluorescence microscopy, the organization and distribution of the cytoplasmic actomyosin fibrils in the fragments changed in synchrony with the contraction cycle. The fibrils formed during the contraction ph

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Gavara, Núria, Raimon Sunyer, Pere Roca-Cusachs, Ramon Farré, Mar Rotger, and Daniel Navajas. "Thrombin-induced contraction in alveolar epithelial cells probed by traction microscopy." Journal of Applied Physiology 101, no. 2 (2006): 512–20. http://dx.doi.org/10.1152/japplphysiol.00185.2006.

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Contractile tension of alveolar epithelial cells plays a major role in the force balance that regulates the structural integrity of the alveolar barrier. The aim of this work was to study thrombin-induced contractile forces of alveolar epithelial cells. A549 alveolar epithelial cells were challenged with thrombin, and time course of contractile forces was measured by traction microscopy. The cells exhibited basal contraction with total force magnitude 55.0 ± 12.0 nN (mean ± SE, n = 12). Traction forces were exerted predominantly at the cell periphery and pointed to the cell center. Thrombin (1

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Cheffings, Thomas H., Nigel J. Burroughs, and Mohan K. Balasubramanian. "Actin turnover ensures uniform tension distribution during cytokinetic actomyosin ring contraction." Molecular Biology of the Cell 30, no. 8 (2019): 933–41. http://dx.doi.org/10.1091/mbc.e18-08-0511.

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In many eukaryotes, cytokinesis is facilitated by the contraction of an actomyosin ring (AMR). The exact mechanisms that lead to this contractility are unknown, although some models posit that actin turnover in the AMR is essential. The effect of reduced actin dynamics during AMR formation has been well studied in Schizosaccharomyces pombe; however, the corresponding effects on AMR contraction are not well understood. By using mutants of the fission yeast actin severing protein Adf1, we observed that contracting AMRs display a “peeling” phenotype, where bundles of actin and myosin peel off fro

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Lippincott, John, and Rong Li. "Dual Function of Cyk2, a cdc15/PSTPIP Family Protein, in Regulating Actomyosin Ring Dynamics and Septin Distribution." Journal of Cell Biology 143, no. 7 (1998): 1947–60. http://dx.doi.org/10.1083/jcb.143.7.1947.

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We previously showed that the budding yeast Saccharomyces cerevisiae assembles an actomyosin-based ring that undergoes a contraction-like size change during cytokinesis. To learn more about the biochemical composition and activity of this ring, we have characterized the in vivo distribution and function of Cyk2p, a budding yeast protein that exhibits significant sequence similarity to the cdc15/PSTPIP family of cleavage furrow proteins. Video microscopy of cells expressing green fluorescent protein (GFP)-tagged Cyk2p revealed that Cyk2p forms a double ring that coincides with the septins throu

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Warren, Gordon L., Jay H. Williams, Christopher W. Ward, et al. "Decreased contraction economy in mouse EDL muscle injured by eccentric contractions." Journal of Applied Physiology 81, no. 6 (1996): 2555–64. http://dx.doi.org/10.1152/jappl.1996.81.6.2555.

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Warren III, Gordon L., Jay H. Williams, Christopher W. Ward, Hideki Matoba, Christopher P. Ingalls, Karl M. Hermann, and R. B. Armstrong. Decreased contraction economy in mouse EDL muscle injured by eccentric contractions. J. Appl. Physiol. 81(6): 2555–2564, 1996.—The objective of this study was to find out whether basal and/or active energy metabolism are altered in isolated mouse extensor digitorum longus muscle injured by eccentric (Ecc) contractions. Measurements of basal O2 consumption and isometric tetanus O2 recovery cost were made at 25°C on muscles that had done either 10 Ecc, 10 isom

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Sechi, Stefano, Anna Frappaolo, Roberta Fraschini, et al. "Rab1 interacts with GOLPH3 and controls Golgi structure and contractile ring constriction during cytokinesis in Drosophila melanogaster." Open Biology 7, no. 1 (2017): 160257. http://dx.doi.org/10.1098/rsob.160257.

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Cytokinesis requires a tight coordination between actomyosin ring constriction and new membrane addition along the ingressing cleavage furrow. However, the molecular mechanisms underlying vesicle trafficking to the equatorial site and how this process is coupled with the dynamics of the contractile apparatus are poorly defined. Here we provide evidence for the requirement of Rab1 during cleavage furrow ingression in cytokinesis. We demonstrate that the gene omelette ( omt ) encodes the Drosophila orthologue of human Rab1 and is required for successful cytokinesis in both mitotic and meiotic di

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Vallen, Elizabeth A., Juliane Caviston, and Erfei Bi. "Roles of Hof1p, Bni1p, Bnr1p, and Myo1p in Cytokinesis inSaccharomyces cerevisiae." Molecular Biology of the Cell 11, no. 2 (2000): 593–611. http://dx.doi.org/10.1091/mbc.11.2.593.

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Cytokinesis in Saccharomyces cerevisiae occurs by the concerted action of the actomyosin system and septum formation. Here we report on the roles of HOF1,BNI1, and BNR1 in cytokinesis, focusing on Hof1p. Deletion of HOF1 causes a temperature-sensitive defect in septum formation. A Hof1p ring forms on the mother side of the bud neck in G2/M, followed by the formation of a daughter-side ring. Around telophase, Hof1p is phosphorylated and the double rings merge into a single ring that contracts slightly and may colocalize with the actomyosin structure. Upon septum formation, Hof1p splits into two

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Mehta, Dolly, Dale D. Tang, Ming-Fang Wu, Simon Atkinson, and Susan J. Gunst. "Role of Rho in Ca2+-insensitive contraction and paxillin tyrosine phosphorylation in smooth muscle." American Journal of Physiology-Cell Physiology 279, no. 2 (2000): C308—C318. http://dx.doi.org/10.1152/ajpcell.2000.279.2.c308.

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We investigated whether Rho activation is required for Ca2+-insensitive paxillin phosphorylation, myosin light chain (MLC) phosphorylation, and contraction in tracheal muscle. Tyrosine-phosphorylated proteins have been implicated in the Ca2+-insensitive contractile activation of smooth muscle tissues. The contractile activation of tracheal smooth muscle increases tyrosine phosphorylation of the cytoskeletal proteins paxillin and focal adhesion kinase. Paxillin is implicated in integrin-mediated signal transduction pathways that regulate cytoskeletal organization and cell motility. In fibroblas

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Yoshinaga, Natsuhiko, and Philippe Marcq. "Contraction of cross-linked actomyosin bundles." Physical Biology 9, no. 4 (2012): 046004. http://dx.doi.org/10.1088/1478-3975/9/4/046004.

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Julien, Jean-Daniel, and Karen Alim. "Oscillatory fluid flow drives scaling of contraction wave with system size." Proceedings of the National Academy of Sciences 115, no. 42 (2018): 10612–17. http://dx.doi.org/10.1073/pnas.1805981115.

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Flows over remarkably long distances are crucial to the functioning of many organisms, across all kingdoms of life. Coordinated flows are fundamental to power deformations, required for migration or development, or to spread resources and signals. A ubiquitous mechanism to generate flows, particularly prominent in animals and amoebas, is actomyosin cortex-driven mechanical deformations that pump the fluid enclosed by the cortex. However, it is unclear how cortex dynamics can self-organize to give rise to coordinated flows across the largely varying scales of biological systems. Here, we develo

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Schmidt, Martin, Blair Bowers, Archana Varma, Dong-Hyun Roh, and Enrico Cabib. "In budding yeast, contraction of the actomyosin ring and formation of the primary septum at cytokinesis depend on each other." Journal of Cell Science 115, no. 2 (2002): 293–302. http://dx.doi.org/10.1242/jcs.115.2.293.

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Saccharomyces cerevisiae chs2 mutants are unable to synthesize primary septum chitin, and myo1 mutants cannot construct a functional contractile ring. The morphology of the two mutants, as observed by electron microscopy, is very similar. In both cases, neither an invagination of the plasma membrane, which normally results from contraction of the actomyosin ring, nor generation of a chitin disc, the primary septum, is observed. Rather, both mutants are able to complete cytokinesis by an abnormal process in which lateral walls thicken gradually and finally meet over an extended region, giving r

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Wirshing, Alison C. E., and Erin J. Cram. "Spectrin regulates cell contractility through production and maintenance of actin bundles in theCaenorhabditis elegansspermatheca." Molecular Biology of the Cell 29, no. 20 (2018): 2433–49. http://dx.doi.org/10.1091/mbc.e18-06-0347.

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Disruption to the contractility of cells, including smooth muscle cells of the cardiovascular system and myoepithelial cells of the glandular epithelium, contributes to the pathophysiology of contractile tissue diseases, including asthma, hypertension, and primary Sjögren’s syndrome. Cell contractility is determined by myosin activity and actomyosin network organization and is mediated by hundreds of protein–protein interactions, many directly involving actin. Here we use a candidate RNA interference screen of more than 100 Caenorhabditis elegans genes with predicted actin-binding and regulato

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Vogel, Sven K., Christian Wölfer, Diego A. Ramirez-Diaz, Robert J. Flassig, Kai Sundmacher, and Petra Schwille. "Symmetry Breaking and Emergence of Directional Flows in Minimal Actomyosin Cortices." Cells 9, no. 6 (2020): 1432. http://dx.doi.org/10.3390/cells9061432.

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Cortical actomyosin flows, among other mechanisms, scale up spontaneous symmetry breaking and thus play pivotal roles in cell differentiation, division, and motility. According to many model systems, myosin motor-induced local contractions of initially isotropic actomyosin cortices are nucleation points for generating cortical flows. However, the positive feedback mechanisms by which spontaneous contractions can be amplified towards large-scale directed flows remain mostly speculative. To investigate such a process on spherical surfaces, we reconstituted and confined initially isotropic minima

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Descovich, Carlos Patino, Daniel B. Cortes, Sean Ryan, et al. "Cross-linkers both drive and brake cytoskeletal remodeling and furrowing in cytokinesis." Molecular Biology of the Cell 29, no. 5 (2018): 622–31. http://dx.doi.org/10.1091/mbc.e17-06-0392.

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Cell shape changes such as cytokinesis are driven by the actomyosin contractile cytoskeleton. The molecular rearrangements that bring about contractility in nonmuscle cells are currently debated. Specifically, both filament sliding by myosin motors, as well as cytoskeletal cross-linking by myosins and nonmotor cross-linkers, are thought to promote contractility. Here we examined how the abundance of motor and nonmotor cross-linkers affects the speed of cytokinetic furrowing. We built a minimal model to simulate contractile dynamics in the Caenorhabditis elegans zygote cytokinetic ring. This mo

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