scholarly journals Suspensor Development in Gagea Lutea (L.) Ker Gawl., with Emphasis on the Cytoskeleton

2015 ◽  
Vol 56 (2) ◽  
pp. 79-90 ◽  
Author(s):  
Joanna Świerczyńska ◽  
Jerzy Bohdanowicz
Keyword(s):  
Fluorescence Microscopy ◽  
Basal Cell ◽  
Actin Filaments ◽  
Early Phase ◽  
Cortical Network ◽  
Dense Network ◽  
Cell Cytoplasm ◽  
Embryo Suspensor ◽  
Gagea Lutea ◽  
Nucleus Surface

Abstract The study used fluorescence microscopy to examine changes in cytoskeleton configuration during development of the embryo suspensor in Gagea lutea and to describe them in tandem with the development of the embryo proper. During the early phase of embryo suspensor development, tubulin and actin filaments were observed in the cytoplasm of the basal cell from the micropylar to the chalazal ends of the cell. Around the nucleus of the basal cell were clusters of numerous microtubules. These accumulations of tubulin arrays congregated near the nucleus surface; numerous bundles of microtubules radiated from the nucleus envelope. At this time, microfil-aments formed a delicate network in the cytoplasm of the basal cell. In the fully differentiated embryo suspensor, microtubules were observed at the chalazal end of the basal cell. Numerous bundles of microtubules were visualized in the cytoplasm adjacent to the wall separating the basal cell from the embryo proper. Microfilaments formed a dense network which uniformly filled the basal cell cytoplasm. There were some foci of F-actin material in the vicinity of the nucleus surface and at the chalazal end of the basal cell. In all studied phases of embryo suspensor development a prominent cortical network of actin and tubulin skeleton was observed in embryo proper cells.

scholarly journals Alisma plantago-aquatica L.: the cytoskeleton of the suspensor development

2014 ◽  
Vol 83 (2) ◽  
pp. 159-166 ◽  
Author(s):  
Joanna Świerczyńska ◽  
Jerzy Bohdanowicz
Keyword(s):  
Basal Cell ◽  
Early Stage ◽  
Cell Development ◽  
Mature Stage ◽  
Rhodamine Phalloidin ◽  
Cytoskeleton Organization ◽  
Stage Of Development ◽  
Embryo Suspensor ◽  
Embryo Cells ◽  
Nucleus Surface

The actin and the tubulin cytoskeleton organization during the differentiation of the embryo-suspensor in <em>Alisma plantago-aquatica</em> was studied in comparison with the development of embryo, using immunofluorescence detection and rhodamine-phalloidin assay. At the early stage of the suspensor basal cell development (from 2- to ~10-celled embryos) microfilaments form an abundant network in the cytoplasm of the basal cell, while the microtubules form a delicate network. At the mature stage of development (from a dozen to several dozen-celled embryos), in the suspensor basal cell, the microfilaments and microtubules were localized from micropylar to chalazal pole of the cell. At the micropylar end of the basal cell a high amount of actin and tubulin material was observed. The microfilaments were mainly arranged parallel whereas numerous bundles of microtubules distributed longitudinally or transversally to the long axis of the cell. At this stage of basal cell functioning, some bundles of microtubules appeared to pass close to the nucleus surface. Microtubules were also observed distributed at the chalazal pole of the basal cell. At the senescence stage of the suspensor basal cell (&gt;100-celled embryos) the actin and tubulin filaments disorganize, some disrupted microfilaments and microtubules were observed in the cytoplasm of the basal cell. At all stages of the suspensor basal cell development in the embryo cells an extensive actin and tubulin network was observed.

3-D examination of the cytoskeletal sheets of mammalian eggs

1992 ◽  
Vol 50 (1) ◽  
pp. 914-915
Author(s):  
Carolyn A. Larabell ◽  
David G. Capco ◽  
G. Ian Gallicano ◽  
Robert W. McGaughey ◽  
Karsten Dierksen ◽  
...  
Keyword(s):  
Actin Filaments ◽  
Somatic Cells ◽  
Freeze Fracture ◽  
Blastocyst Stage ◽  
Cell Cytoplasm ◽  
Planar Structures ◽  
Cytoskeletal Network ◽  
Entire Cell ◽  
Cytoskeletal Networks ◽  
Mammalian Eggs

Mammalian eggs and embryos contain an elaborate cytoskeletal network of “sheets” which are distributed throughout the entire cell cytoplasm. Cytoskeletal sheets are long, planar structures unlike the cytoskeletal networks typical of somatic cells (actin filaments, microtubules, and intermediate filaments), which are filamentous. These sheets are not found in mammalian somatic cells nor are they found in nonmammalian eggs or embryos. Evidence that they are, indeed, cytoskeletal in nature is derived from studies demonstrating that 1) the sheets are retained in the detergent-resistant cytoskeleton fraction; 2) there are no associated membranes (determined by freeze-fracture); and 3) the sheets dissociate into filaments at the blastocyst stage of embryogenesis. Embedment-free sections of hamster eggs viewed at 60 kV show sheets running across the egg cytoplasm (Fig. 1). Although this approach provides excellent global views of the sheets and their reorganization during development, the mechanism of image formation for embedment-free sections does not permit evaluation of the sheets at high resolution.

scholarly journals Stress fibers are embedded in a contractile cortical network

2020 ◽  
Author(s):  
Timothée Vignaud ◽  
Calina Copos ◽  
Christophe Leterrier ◽  
Qingzong Tseng ◽  
Laurent Blanchoin ◽  
...  
Keyword(s):  
Cell Fate ◽  
Actin Filaments ◽  
Mechanical Response ◽  
Force Production ◽  
Traction Force ◽  
Cortical Network ◽  
Cortical Actin ◽  
Cell Fate Decisions ◽  
Production And Distribution ◽  
Intracellular Forces

ABSTRACTContractile actomyosin networks generate intracellular forces essential for the regulation of cell shape, migration, and cell-fate decisions, ultimately leading to the remodeling and patterning of tissues. Although actin filaments aligned in bundles represent the main source of traction-force production in adherent cells, there is increasing evidence that these bundles form interconnected and interconvertible structures with the rest of the intracellular actin network. In this study, we explored how these bundles are connected to the surrounding cortical network and the mechanical impact of these interconnected structures on the production and distribution of traction forces on the extracellular matrix and throughout the cell. By using a combination of hydrogel micropatterning, traction-force microscopy and laser photoablation, we measured the relaxation of the cellular traction field in response to local photoablations at various positions within the cell. Our experimental results and modeling of the mechanical response of the network revealed that bundles were fully embedded along their entire length in a continuous and contractile network of cortical filaments. Moreover, the propagation of the contraction of these bundles throughout the entire cell was dependent on this embedding. In addition, these bundles appeared to originate from the alignment and coalescence of thin and unattached cortical actin filaments from the surrounding mesh.

Development of hypersynchrony in the cortical network during chemoconvulsant-induced epileptic seizures in vivo

2012 ◽  
Vol 107 (6) ◽  
pp. 1718-1730 ◽  
Author(s):  
Adi Cymerblit-Sabba ◽  
Yitzhak Schiller
Keyword(s):  
Action Potential ◽  
Early Phase ◽  
Epileptic Seizures ◽  
Firing Frequency ◽  
Cortical Network ◽  
Small Subset ◽  
Action Potential Firing ◽  
Neuronal Synchronization ◽  
Potential Firing

The prevailing view of epileptic seizures is that they are caused by increased hypersynchronous activity in the cortical network. However, this view is based mostly on electroencephalography (EEG) recordings that do not directly monitor neuronal synchronization of action potential firing. In this study, we used multielectrode single-unit recordings from the hippocampus to investigate firing of individual CA1 neurons and directly monitor synchronization of action potential firing between neurons during the different ictal phases of chemoconvulsant-induced epileptic seizures in vivo. During the early phase of seizures manifesting as low-amplitude rhythmic β-electrocorticography (ECoG) activity, the firing frequency of most neurons markedly increased. To our surprise, the average overall neuronal synchronization as measured by the cross-correlation function was reduced compared with control conditions with ∼60% of neuronal pairs showing no significant correlated firing. However, correlated firing was not uniform and a minority of neuronal pairs showed a high degree of correlated firing. Moreover, during the early phase of seizures, correlated firing between 9.8 ± 5.1% of all stably recorded pairs increased compared with control conditions. As seizures progressed and high-frequency ECoG polyspikes developed, the firing frequency of neurons further increased and enhanced correlated firing was observed between virtually all neuronal pairs. These findings indicated that epileptic seizures represented a hyperactive state with widespread increase in action potential firing. Hypersynchrony also characterized seizures. However, it initially developed in a small subset of neurons and gradually spread to involve the entire cortical network only in the later more intense ictal phases.

scholarly journals Coarse-grained simulations of actomyosin rings point to a nodeless model involving both unipolar and bipolar myosins

2017 ◽  
Author(s):  
Lam T. Nguyen ◽  
Matthew T. Swulius ◽  
Samya Aich ◽  
Mithilesh Mishra ◽  
Grant J. Jensen
Keyword(s):  
Experimental Data ◽  
Cell Division ◽  
Fluorescence Microscopy ◽  
Actin Filaments ◽  
Coarse Grained ◽  
Eukaryotic Cells ◽  
Ring Assembly ◽  
Assembly Result ◽  
Coarse Grained Simulations ◽  
Electron Cryotomography

AbstractCytokinesis in most eukaryotic cells is orchestrated by a contractile actomyosin ring. While many of the proteins involved are known, the mechanism of constriction remains unclear. Informed by existing literature and new 3D molecular details from electron cryotomography, here we develop 3D coarse-grained models of actin filaments, unipolar and bipolar myosins, actin crosslinkers, and membranes and simulate their nteractions. Exploring a matrix of possible actomyosin configurations suggested that node-based architectures ike those presently described for ring assembly result in membrane puckers not seen in EM images of real cells. Instead, the model that best matches data from fluorescence microscopy, electron cryotomography, and biochemical experiments is one in which actin filaments transmit force to the membrane through evenly-distributed, membrane-attached, unipolar myosins, with bipolar myosins in the ring driving contraction. While at this point this model is only favored (not proven), the work highlights the power of coarse-grained biophysical simulations to compare complex mechanistic hypotheses.Significance StatementIn most eukaryotes, a ring of actin and myosin drives cell division, but how the elements of the ring are arranged and constrict remain unclear. Here we use 3D coarse-grained simulations to explore various possibilities. Our simulations suggest that if actomyosin is arranged in nodes (as suggested by a popular model of ring assembly), the membrane distorts in ways not seen experimentally. Instead, actin and myosin are more ikely uniformly distributed around the ring. In the model that best fits experimental data, ring tension is generated by interactions between bipolar myosins and actin, and transmitted to the membrane via unipolar myosins. Technologically the study highlights how coarse-grained simulations can test specific mechanistic hypotheses by comparing their predicted outcomes to experimental results.

scholarly journals Synergy between Wsp1 and Dip1 may initiate assembly of endocytic actin networks

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Connor J Balzer ◽  
Michael L James ◽  
Heidy Y Narvaez-Ortiz ◽  
Luke A Helgeson ◽  
Vladimir Sirotkin ◽  
...  
Keyword(s):  
Fluorescence Microscopy ◽  
Schizosaccharomyces Pombe ◽  
Actin Filament ◽  
Single Molecule ◽  
Actin Filaments ◽  
Total Internal Reflection ◽  
Actin Assembly ◽  
Actin Network ◽  
Actin Networks ◽  
Co Activation

The actin filament nucleator Arp2/3 complex is activated at cortical sites in Schizosaccharomyces pombe to assemble branched actin networks that drive endocytosis. Arp2/3 complex activators Wsp1 and Dip1 are required for proper actin assembly at endocytic sites, but how they coordinately control Arp2/3-mediated actin assembly is unknown. Alone, Dip1 activates Arp2/3 complex without preexisting actin filaments to nucleate ‘seed’ filaments that activate Wsp1-bound Arp2/3 complex, thereby initiating branched actin network assembly. In contrast, because Wsp1 requires preexisting filaments to activate, it has been assumed to function exclusively in propagating actin networks by stimulating branching from preexisting filaments. Here we show that Wsp1 is important not only for propagation but also for initiation of endocytic actin networks. Using single molecule total internal reflection fluorescence microscopy we show that Wsp1 synergizes with Dip1 to co-activate Arp2/3 complex. Synergistic co-activation does not require preexisting actin filaments, explaining how Wsp1 contributes to actin network initiation in cells.

Presence of Clathrin at Adhesion Sites in Phagocytosing Macrophages

1982 ◽  
Vol 40 ◽  
pp. 114-117
Author(s):  
J. Aggeler ◽  
J.E. Heuser ◽  
Z. Werb
Keyword(s):  
Plasma Membrane ◽  
Actin Filaments ◽  
Binding Proteins ◽  
Binding Protein ◽  
Cell Spreading ◽  
Actin Binding ◽  
Dense Network ◽  
Actin Binding Protein ◽  
Adhesion Sites ◽  
Cytoplasmic Surface

Phagocytosis of particles by macrophages may be similar to cell spreading on a substratum, in that a dense network of actin filaments appears beneath the plasma membrane in both cases. When viewed in broken-open or detergent- extracted cells, cytoskeletal filaments are observed to form focal attachments to the plasma membrane and to the cytoplasmic surface of phagosomes. Hartwig et al. have presented a model of phagocytosis in which an actin-binding protein alters the organization of subplasmalemma1 actin filaments in such a way that the plasma membrane is forced up over the particle to form the phagosome. Their evidence indicates that similar actin-binding proteins may function during cell spreading.

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