Academic literature on the topic 'Actomyosine – Contraction'

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Actomyosine – Contraction.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Actomyosine – Contraction"

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.

Full text
Abstract:
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
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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
APA, Harvard, Vancouver, ISO, and other styles
5

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.

Full text
Abstract:
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
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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
APA, Harvard, Vancouver, ISO, and other styles
More sources
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!