Actin in the Green Alga,
            <i>Nitella</i>

Palevitz, Barry A.; Ash, John F.; Hepler, Peter K.

doi:10.1073/pnas.71.2.363

Cited by 158 publications

(51 citation statements)

References 17 publications

(19 reference statements)

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“…5), whereas control cells perfused with NBD-CI and NBD-ethanolamine show no fluorescent cables. Structural features of the actin cable network marked by NBD-Ph in these living cells confirm features previously observed in fixed cells marked with myosin fragments (16)(17)(18).…”

supporting

confidence: 85%

“…The giant cells of characean algae show rapid rotational cytoplasmic streaming. Electron and fluorescence microscopic studies employing myosin fragments have identified subcortical actin cables that are believed to participate in the generation of the streaming in these cells (16)(17)(18). These cables form unambiguous structures attached to the chloroplast files.…”

mentioning

confidence: 99%

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Fluorescence staining of the actin cytoskeleton in living cells with 7-nitrobenz-2-oxa-1,3-diazole-phallacidin.

Barak¹,

Yocum²,

Nothnagel³

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

393

171

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An active fluorescent derivative of the actin-binding mushroom toxin phallacidin has been synthesized. Convenient methods were developed to stain actin cytoskeletal structures in living and fixed cultured animal cells and actively streaming algal cells. Actin binding specificity was demonstrated by competitive binding experiments and comparative staining of well-known structures. Large populations of living animal cells in culture were readily stained by using a relatively mild lysolecithin permeabilization procedure facilitated by the small molecular size of the label. Actin in animal cells was stained stress fibers, ruffles, the cellular geodome, and in diffuse appearing distributions apparently associated with the plasma membrane. Staining of actin cables in algae with nitrobenzoxadiazole (NBD)-phallacidin did not inhibit cytoplasmic streaming. NBD-phallacidin provides a convenient actin-specific fluorescent label for cellular cytoskeletal structures with promise for use in studies of actin dynamics in living systems.

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supporting

confidence: 85%

mentioning

confidence: 99%

Fluorescence staining of the actin cytoskeleton in living cells with 7-nitrobenz-2-oxa-1,3-diazole-phallacidin.

Barak¹,

Yocum²,

Nothnagel³

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

393

171

View full text Add to dashboard Cite

show abstract

“…We expected that if the cytoplasm behaves as an incompressible fluid confined in a container, the anterior-directed cortical shear force would generate countercurrent (posterior-directed) flow in the central region of the cell. In characean algae, while streaming occurs throughout the cell, the driving force for streaming is generated by myosin XI in a layer just beneath the cell surface (4,(16)(17)(18)(19)(20)(21)(22)(23). For characean algae, a hydrodynamic simulation assuming surface myosin as the sole active force generator demonstrated that the force transmitted toward the central cytoplasmic region due to the viscosity of the cytoplasm quantitatively accounts for cytoplasmic streaming (4).…”

mentioning

confidence: 99%

Hydrodynamic property of the cytoplasm is sufficient to mediate cytoplasmic streaming in the Caenorhabiditis elegans embryo

Niwayama

Shinohara

Kimura

2011

Proc. Natl. Acad. Sci. U.S.A.

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Cytoplasmic streaming is a type of intracellular transport widely seen in nature. Cytoplasmic streaming in Caenorhabditis elegans at the one-cell stage is bidirectional; the flow near the cortex ("cortical flow") is oriented toward the anterior, whereas the flow in the central region ("cytoplasmic flow") is oriented toward the posterior. Both cortical flow and cytoplasmic flow depend on non-musclemyosin II (NMY-2), which primarily localizes in the cortex. The manner in which NMY-2 proteins drive cytoplasmic flow in the opposite direction from remote locations has not been fully understood. In this study, we demonstrated that the hydrodynamic properties of the cytoplasm are sufficient to mediate the forces generated by the cortical myosin to drive bidirectional streaming throughout the cytoplasm. We quantified the flow velocities of cytoplasmic streaming using particle image velocimetry (PIV) and conducted a threedimensional hydrodynamic simulation using the moving particle semiimplicit method. Our simulation quantitatively reconstructed the quantified flow velocity distribution resolved through PIV analysis. Furthermore, our PIV analyses detected microtubule-dependent flows during the pronuclear migration stage. These flows were reproduced via hydrodynamic interactions between moving pronuclei and the cytoplasm. The agreement of flow dynamics in vivo and in simulation indicates that the hydrodynamic properties of the cytoplasm are sufficient to mediate cytoplasmic streaming in C. elegans embryos. fluid dynamics | particle method | Newtonian fluid | cell polarity | algae

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“…It goes up along one hemicylinder to the node and comes down along the other. More than 30 years ago, it has been discovered that such a course was related to the orientation of actin bundles and their AF subunits [Kersey, 1974;Palevitz et al, 1974;Palevitz and Hepler, 1975;Kersey et al, 1976]. Indeed, actin bundles align with the cytosplasmic flow and contain AFs arranged with the same polarity, i.e.…”

Section: Actin Bundles In Cytoplasmic Streaming and Transvacuolar Strmentioning

confidence: 99%

Actin bundling in plants

Thomas

Tholl

Moes

et al. 2009

Cell Motil. Cytoskeleton

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Tight regulation of plant actin cytoskeleton organization and dynamics is crucial for numerous cellular processes including cell division, expansion and intracellular trafficking. Among the various actin regulatory proteins, actin-bundling proteins trigger the formation of bundles composed of several parallel actin filaments closely packed together. Actin bundles are present in virtually all plant cells, but their biological roles have rarely been addressed directly. However, decades of research in the plant cytoskeleton field yielded a bulk of data from which an overall picture of the functions supplied by actin bundles in plant cells emerges. Although plants lack several equivalents of animal actin-bundling proteins, they do possess major bundler classes including fimbrins, villins and formins. The existence of additional players is not excluded as exemplified by the recent characterization of plant LIM proteins, which trigger the formation of actin bundles both in vitro and in vivo. This apparent functional redundancy likely reflects the need for plant cells to engineer different types of bundles that act at different sub-cellular locations and exhibit specific function-related properties. By surveying information regarding the properties of plant actin bundles and their associated bundling proteins, the present review aims at clarifying why and how plants make actin bundles. Cell Motil. Cytoskeleton 66: 940-957, 2009. '

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Actin in the Green Alga, Nitella

Cited by 158 publications

References 17 publications

Fluorescence staining of the actin cytoskeleton in living cells with 7-nitrobenz-2-oxa-1,3-diazole-phallacidin.

Fluorescence staining of the actin cytoskeleton in living cells with 7-nitrobenz-2-oxa-1,3-diazole-phallacidin.

Hydrodynamic property of the cytoplasm is sufficient to mediate cytoplasmic streaming in the Caenorhabiditis elegans embryo

Actin bundling in plants

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