scholarly journals Network Contractility during Cytokinesis—From Molecular to Global Views

Biomolecules ◽  
2019 ◽  
Vol 9 (5) ◽  
pp. 194 ◽  
Author(s):  
Joana Leite ◽  
Daniel Sampaio Osorio ◽  
Ana Filipa Sobral ◽  
Ana Marta Silva ◽  
Ana Xavier Carvalho
Keyword(s):  
Motor Activity ◽  
Network Architecture ◽  
Theoretical Models ◽  
Coarse Grained ◽  
Cell Cortex ◽  
Contractile Ring ◽  
Daughter Cells ◽  
Experimental Approaches ◽  
Global Understanding ◽  
Last Stage

Cytokinesis is the last stage of cell division, which partitions the mother cell into two daughter cells. It requires the assembly and constriction of a contractile ring that consists of a filamentous contractile network of actin and myosin. Network contractility depends on network architecture, level of connectivity and myosin motor activity, but how exactly is the contractile ring network organized or interconnected and how much it depends on motor activity remains unclear. Moreover, the contractile ring is not an isolated entity; rather, it is integrated into the surrounding cortex. Therefore, the mechanical properties of the cell cortex and cortical behaviors are expected to impact contractile ring functioning. Due to the complexity of the process, experimental approaches have been coupled to theoretical modeling in order to advance its global understanding. While earlier coarse-grained descriptions attempted to provide an integrated view of the process, recent models have mostly focused on understanding the behavior of an isolated contractile ring. Here we provide an overview of the organization and dynamics of the actomyosin network during cytokinesis and discuss existing theoretical models in light of cortical behaviors and experimental evidence from several systems. Our view on what is missing in current models and should be tested in the future is provided.

scholarly journals Rap1-dependent pathways coordinate cytokinesis in Dictyostelium

2014 ◽  
Vol 25 (25) ◽  
pp. 4195-4204 ◽  
Author(s):  
Katarzyna Plak ◽  
Ineke Keizer-Gunnink ◽  
Peter J. M. van Haastert ◽  
Arjan Kortholt
Keyword(s):  
Cell Division ◽  
Cell Cortex ◽  
Adherent Cells ◽  
Contractile Ring ◽  
Daughter Cells ◽  
Small G Protein ◽  
Rap1 Activation ◽  
Actomyosin Cytoskeleton ◽  
Mutant Cells ◽  
Severe Growth

Cytokinesis is the final step of mitosis when a mother cell is separated into two daughter cells. Major cytoskeletal changes are essential for cytokinesis; it is, however, not well understood how the microtubules and actomyosin cytoskeleton are exactly regulated in time and space. In this paper, we show that during the early stages of cytokinesis, in rounded-up Dictyostelium discoideum cells, the small G-protein Rap1 is activated uniformly at the cell cortex. When cells begin to elongate, active Rap1 becomes restricted from the furrow region, where the myosin contractile ring is subsequently formed. In the final stages of cytokinesis, active Rap1 is only present at the cell poles. Mutant cells with decreased Rap1 activation at the poles showed strongly decreased growth rates. Hyperactivation of Rap1 results in severe growth delays and defective spindle formation in adherent cells and cell death in suspension. Furthermore, Rap mutants show aberrant regulation of the actomyosin cytoskeleton, resulting in extended furrow ingression times and asymmetrical cell division. We propose that Rap1 drives cytokinesis progression by coordinating the three major cytoskeletal components: microtubules, actin, and myosin II. Importantly, mutated forms of Rap also affect cytokinesis in other organisms, suggesting a conserved role for Rap in cell division.

scholarly journals Mechanism of the formation of contractile ring in dividing cultured animal cells. II. Cortical movement of microinjected actin filaments.

1990 ◽  
Vol 111 (5) ◽  
pp. 1905-1911 ◽  
Author(s):  
L G Cao ◽  
Y L Wang
Keyword(s):  
Actin Filaments ◽  
Average Rate ◽  
Rat Kidney ◽  
Equatorial Region ◽  
Cell Cortex ◽  
Polar Regions ◽  
Cortical Actin ◽  
Animal Cells ◽  
Contractile Ring ◽  
Directional Movement

The contractile ring in dividing animal cells is formed primarily through the reorganization of existing actin filaments (Cao, L.-G., and Y.-L. Wang. 1990. J. Cell Biol. 110:1089-1096), but it is not clear whether the process involves a random recruitment of diffusible actin filaments from the cytoplasm, or a directional movement of cortically associated filaments toward the equator. We have studied this question by observing the distribution of actin filaments that have been labeled with fluorescent phalloidin and microinjected into dividing normal rat kidney (NRK) cells. The labeled filaments are present primarily in the cytoplasm during prometaphase and early metaphase, but become associated extensively with the cell cortex 10-15 min before the onset of anaphase. This process is manifested both as an increase in cortical fluorescence intensity and as movements of discrete aggregates of actin filaments toward the cortex. The concentration of actin fluorescence in the equatorial region, accompanied by a decrease of fluorescence in polar regions, is detected 2-3 min after the onset of anaphase. By directly tracing the distribution of aggregates of labeled actin filaments, we are able to detect, during anaphase and telophase, movements of cortical actin filaments toward the equator at an average rate of 1.0 micron/min. Our results, combined with previous observations, suggest that the organization of actin filaments during cytokinesis probably involves an association of cytoplasmic filaments with the cortex, a movement of cortical filaments toward the cleavage furrow, and a dissociation of filaments from the equatorial cortex.

scholarly journals Fission yeast myosin Myo2 is down-regulated in actin affinity by light chain phosphorylation

2017 ◽  
Vol 114 (35) ◽  
pp. E7236-E7244 ◽  
Author(s):  
Luther W. Pollard ◽  
Carol S. Bookwalter ◽  
Qing Tang ◽  
Elena B. Krementsova ◽  
Kathleen M. Trybus ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Light Chain ◽  
Force Production ◽  
Class Ii ◽  
Cell System ◽  
Cell Cortex ◽  
Animal Cells ◽  
Contractile Ring ◽  
Biophysical Studies

Studies in fission yeast Schizosaccharomyces pombe have provided the basis for the most advanced models of the dynamics of the cytokinetic contractile ring. Myo2, a class-II myosin, is the major source of tension in the contractile ring, but how Myo2 is anchored and regulated to produce force is poorly understood. To enable more detailed biochemical/biophysical studies, Myo2 was expressed in the baculovirus/Sf9 insect cell system with its two native light chains, Rlc1 and Cdc4. Milligram yields of soluble, unphosphorylated Myo2 were obtained that exhibited high actin-activated ATPase activity and in vitro actin filament motility. The fission yeast specific chaperone Rng3 was thus not required for expression or activity. In contrast to nonmuscle myosins from animal cells that require phosphorylation of the regulatory light chain for activation, phosphorylation of Rlc1 markedly reduced the affinity of Myo2 for actin. Another unusual feature of Myo2 was that, unlike class-II myosins, which generally form bipolar filamentous structures, Myo2 showed no inclination to self-assemble at approximately physiological salt concentrations, as analyzed by sedimentation velocity ultracentrifugation. This lack of assembly supports the hypothesis that clusters of Myo2 depend on interactions at the cell cortex in structural units called nodes for force production during cytokinesis.

scholarly journals Polar relaxation by dynein-mediated removal of cortical myosin II

2020 ◽  
Vol 219 (8) ◽  
Author(s):  
Bernardo Chapa-y-Lazo ◽  
Motonari Hamanaka ◽  
Alexander Wray ◽  
Mohan K. Balasubramanian ◽  
Masanori Mishima
Keyword(s):  
Recent Work ◽  
Molecular Mechanism ◽  
Molecular Mechanisms ◽  
Myosin Ii ◽  
Cell Cortex ◽  
Cleavage Furrow ◽  
Contractile Ring ◽  
C Elegans ◽  
Polar Cell

Nearly six decades ago, Lewis Wolpert proposed the relaxation of the polar cell cortex by the radial arrays of astral microtubules as a mechanism for cleavage furrow induction. While this mechanism has remained controversial, recent work has provided evidence for polar relaxation by astral microtubules, although its molecular mechanisms remain elusive. Here, using C. elegans embryos, we show that polar relaxation is achieved through dynein-mediated removal of myosin II from the polar cortexes. Mutants that position centrosomes closer to the polar cortex accelerated furrow induction, whereas suppression of dynein activity delayed furrowing. We show that dynein-mediated removal of myosin II from the polar cortexes triggers a bidirectional cortical flow toward the cell equator, which induces the assembly of the actomyosin contractile ring. These results provide a molecular mechanism for the aster-dependent polar relaxation, which works in parallel with equatorial stimulation to promote robust cytokinesis.

A centrosome-associated antibody from Drosophila melanogaster reveals a new microtubule-dependent structure in the equatorial zone of Parascaris univalens embryos

1993 ◽  
Vol 106 (3) ◽  
pp. 719-730
Author(s):  
M. Jimenez ◽  
C. Goday
Keyword(s):  
Drosophila Melanogaster ◽  
Cytochalasin B ◽  
Cell Communication ◽  
Equatorial Zone ◽  
Contractile Ring ◽  
Daughter Cells ◽  
Ring Assembly ◽  
Single Body ◽  
A Cell ◽  
Cycle Dependent

The distribution of antigens to two antibodies (Bx63 and Rb188) that associate to Drosophila melanogaster centrosomes has been investigated in the nematode Parascaris. By western blot analysis both antibodies identify in Parascaris polypeptides of the same molecular mass as in Drosophila (Rb188 a 185 kDa antigen and Bx63 185 kDa and 66 kDa antigens). By immunocytochemistry we show that the centrosomes of Parascaris contain the 185 kDa antigen recognized by polyclonal Rb188 and monoclonal Bx63 antibodies. In addition, Bx63 reveals cytoplasmic midzone structures, not found in Drosophila, that display a cell cycle-dependent organization in embryos. These structures, which most probably contain the 66 kDa antigen revealed by Bx63, appear at the onset of anaphase as fibrillar-like structures that during anaphase form a ring-like structure encircling the equatorial plane of the blastomere. Before furrowing, the antigen participates in the formation of the midbody and associates with convergent polar microtubules. After blastomere division, Bx63 signal persists as a single body between the daughter cells. The analysis of chilled and nocodazole-treated embryos suggests that the localization of the midzone Bx63 antigen is dependent on non-kinetochore microtubules. Inhibition of furrowing by cytochalasin B shows that the antigen persists after the disassembly of microfilaments. Cytological observations of contractile ring and Bx63 ring assembly indicate that both structures do not simultaneously colocalize at the equatorial zone. The data suggest a spindle-dependent distribution of the Bx63 antigen during cytokinesis. We discuss the participation of this antigen in the organization of the midbody before furrowing, and consider the possible relevance of the midbody with respect to cell to cell communication during early development in nematodes.

scholarly journals Actin Network Architecture Can Determine Myosin Motor Activity

Science ◽  
2012 ◽  
Vol 336 (6086) ◽  
pp. 1310-1314 ◽  
Author(s):  
A.-C. Reymann ◽  
R. Boujemaa-Paterski ◽  
J.-L. Martiel ◽  
C. Guerin ◽  
W. Cao ◽  
...  
Keyword(s):  
Motor Activity ◽  
Network Architecture ◽  
Actin Network ◽  
Myosin Motor

On the role of enemies in divergence and diversification of prey: a review and synthesis

2005 ◽  
Vol 83 (7) ◽  
pp. 894-910 ◽  
Author(s):  
Steven M Vamosi
Keyword(s):  
Visual Cues ◽  
Phenotypic Diversity ◽  
Theoretical Models ◽  
Ecological Interactions ◽  
Closely Related Species ◽  
Diversification Rates ◽  
Extinction Rates ◽  
Phenotypic Divergence ◽  
Experimental Approaches

Understanding the contribution of ecological interactions to the origin and maintenance of diversity is a fundamental challenge for ecologists and evolutionary biologists, and one that is currently receiving a great deal of attention. Natural enemies (e.g., predators, parasites, and herbivores) are ubiquitous in food webs and are predicted to have significant impacts on phenotypic diversity and on speciation, and extinction rates of their prey. Spurred by the development of a theoretical framework beginning in the late 1970s, there is now a growing body of literature that addresses the effects of enemy–prey interactions on the evolution of prey. A number of theoretical models predict that enemies can produce phenotypic divergence between closely related species, even in the absence of interspecific competition for resources. Effects on diversification of prey are more variable, and enemies may either enhance or depress speciation and extinction rates of their prey. Empirical evidences from a number of study systems, notably those involving predators and prey in aquatic environments and interactions between insects and flowering plants, confirm both predictions. There is now considerable evidence for the role of enemies, especially those that are size-selective or use visual cues when identifying suitable prey, on phenotypic divergence of sympatric and allopatric taxa. Enemies may spur diversification rates in certain groups under some circumstances, and hinder diversification rates in other cases. I suggest that further research should focus on the role of enemies in diversification of prey, with significant insights likely to be the product of applying traditional experimental approaches and emerging comparative phylogenetic methods.

Cavitation Behavior of Ultra-Fine Grained Ti-6Al-4V Alloy Produced by Equal-Channel Angular Pressing

2007 ◽  
Vol 551-552 ◽  
pp. 621-626
Author(s):  
Young Gun Ko ◽  
Yong Nam Kwon ◽  
Jung Hwan Lee ◽  
Dong Hyuk Shin ◽  
Chong Soo Lee
Keyword(s):  
Grain Size ◽  
Strain Rate ◽  
Equal Channel Angular Pressing ◽  
Cavity Growth ◽  
Rate Sensitivity ◽  
Theoretical Models ◽  
Coarse Grained ◽  
Fine Grained ◽  
Angular Pressing ◽  
Cavitation Behavior

Cavitation behavior during superplastic flow of ultra-fine grained (UFG) Ti-6Al-4V alloy was established with the variation of grain size and misorientation. After imposing an effective strainup to 8 via equal-channel angular pressing (ECAP) at 873 K, alpha-phase grains were markedly refined from 11 μm to ≈ 0.3 μm, and misorientation angle was increased. Uniaxial-tension tests were conducted for initial coarse grained (CG) and two UFG alloys (ε = 4 and 8) at temperature of 973 K and strain rate of 10-4 s-1. Quantitative measurements of cavitation evidenced that both the average size and the area fraction of cavities significantly decreased with decreasing grain size and/or increasing misorientation. It was also found that, when compared to CG alloy, cavitation as well as diffused necking was less prevalent in UFG alloys, which was presumably due to the higher value of strain-rate sensitivity. Based on the several theoretical models describing the cavity growth behavior, the cavity growth mechanism in UFG alloys was suggested.

scholarly journals Fascetto interacting protein ensures proper cytokinesis and ploidy

2019 ◽  
Vol 30 (8) ◽  
pp. 992-1007 ◽  
Author(s):  
Zachary T. Swider ◽  
Rachel K. Ng ◽  
Ramya Varadarajan ◽  
Carey J. Fagerstrom ◽  
Nasser M. Rusan
Keyword(s):  
Cell Division ◽  
Tissue Repair ◽  
Complete Separation ◽  
Contractile Ring ◽  
Interacting Protein ◽  
Simultaneous Reduction ◽  
Central Spindle ◽  
Daughter Cells ◽  
Molecular Machinery ◽  
The Brain

Cell division is critical for development, organ growth, and tissue repair. The later stages of cell division include the formation of the microtubule (MT)-rich central spindle in anaphase, which is required to properly define the cell equator, guide the assembly of the acto-myosin contractile ring and ultimately ensure complete separation and isolation of the two daughter cells via abscission. Much is known about the molecular machinery that forms the central spindle, including proteins needed to generate the antiparallel overlapping interzonal MTs. One critical protein that has garnered great attention is the protein regulator of cytokinesis 1, or Fascetto (Feo) in Drosophila, which forms a homodimer to cross-link interzonal MTs, ensuring proper central spindle formation and cytokinesis. Here, we report on a new direct protein interactor and regulator of Feo we named Feo interacting protein (FIP). Loss of FIP results in a reduction in Feo localization, rapid disassembly of interzonal MTs, and several defects related to cytokinesis failure, including polyploidization of neural stem cells. Simultaneous reduction in Feo and FIP results in very large, tumorlike DNA-filled masses in the brain that contain hundreds of centrosomes. In aggregate, our data show that FIP acts directly on Feo to ensure fully accurate cell division.

scholarly journals Bud8p and Bud9p, Proteins That May Mark the Sites for Bipolar Budding in Yeast

2001 ◽  
Vol 12 (8) ◽  
pp. 2497-2518 ◽  
Author(s):  
Heidi A. Harkins ◽  
Nicolas Pagé ◽  
Laura R. Schenkman ◽  
Claudio De Virgilio ◽  
Sidney Shaw ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Double Mutant ◽  
Previous Analysis ◽  
Integral Membrane Proteins ◽  
Cell Cortex ◽  
Daughter Cells ◽  
Distal Pole ◽  
Bud Position ◽  
Bud Site ◽  
Hydrophilic Domain

The bipolar budding pattern of a /α Saccharomyces cerevisiae cells appears to depend on persistent spatial markers in the cell cortex at the two poles of the cell. Previous analysis of mutants with specific defects in bipolar budding identifiedBUD8 and BUD9 as potentially encoding components of the markers at the poles distal and proximal to the birth scar, respectively. Further genetic analysis reported here supports this hypothesis. Mutants deleted for BUD8 orBUD9 grow normally but bud exclusively from the proximal and distal poles, respectively, and the double-mutant phenotype suggests that the bipolar budding pathway has been totally disabled. Moreover, overexpression of these genes can cause either an increased bias for budding at the distal (BUD8) or proximal (BUD9) pole or a randomization of bud position, depending on the level of expression. The structures and localizations of Bud8p and Bud9p are also consistent with their postulated roles as cortical markers. Both proteins appear to be integral membrane proteins of the plasma membrane, and they have very similar overall structures, with long N-terminal domains that are both N- andO-glycosylated followed by a pair of putative transmembrane domains surrounding a short hydrophilic domain that is presumably cytoplasmic. The putative transmembrane and cytoplasmic domains of the two proteins are very similar in sequence. When Bud8p and Bud9p were localized by immunofluorescence and tagging with GFP, each protein was found predominantly in the expected location, with Bud8p at presumptive bud sites, bud tips, and the distal poles of daughter cells and Bud9p at the necks of large-budded cells and the proximal poles of daughter cells. Bud8p localized approximately normally in several mutants in which daughter cells are competent to form their first buds at the distal pole, but it was not detected in abni1 mutant, in which such distal-pole budding is lost. Surprisingly, Bud8p localization to the presumptive bud site and bud tip also depends on actin but is independent of the septins.

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