The Motility of Chara corallina Myosin was Inhibited Reversibly by 2,3-Butanedione Monoxime (BDM)

K, Funaki; Nagata, Ayumi; Akimoto, Youka; Shimada, Kiyo; Ito, Kohji; Yamamoto, Keiichi

doi:10.1093/pcp/pch154

Cited by 33 publications

(21 citation statements)

References 31 publications

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“…Treatment with latrunculin B at concentrations that we previously determined could depolymerize cortical actin filaments [Foissner and Wasteneys, 2007], produced inconsistent results in the presence of DiOC 6 . The myosin inhibitors BDM or ML-7 had no effect at the concentrations tested, consistent with other studies showing that they must be used at very high concentrations and are not readily reversible in characean algae [McCurdy, 1999;Funaki et al, 2004].…”

Section: Nem Immobilizes Subcortical and Cortical Ersupporting

confidence: 88%

Microtubule‐dependent motility and orientation of the cortical endoplasmic reticulum in elongating characean internodal cells

Foissner

Menzel

Wasteneys

2009

Cell Motil. Cytoskeleton

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Motility of the endoplasmic reticulum (ER) is predominantly microtubule- dependent in animal cells but thought to be entirely actomyosin-dependent in plant cells. Using live cell imaging and transmission electron microscopy to examine ER motility and structural organization in giant internodal cells of characean algae, we discovered that at the onset of cell elongation, the cortical ER situated near the plasma membrane formed a tight meshwork of predominantly transverse ER tubules that frequently coaligned with microtubules. Microtubule depolymerization increased mesh size and decreased the dynamics of the cortical ER. In contrast, perturbing the cortical actin array with cytochalasins did not affect the transverse orientation but decreased mesh size and increased ER dynamics. Our data suggest that myosin-dependent ER motility is confined to the ER strands in the streaming endoplasm, while the more sedate cortical ER uses microtubule-based mechanisms for organization and motility during early stages of cell elongation. We show further that the ER has an inherent, NEM-sensitive dynamics which can be altered via interaction with the cytoskeleton and that tubule formation and fusion events are cytoskeleton-independent.

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Section: Nem Immobilizes Subcortical and Cortical Ersupporting

confidence: 88%

Microtubule‐dependent motility and orientation of the cortical endoplasmic reticulum in elongating characean internodal cells

Foissner

Menzel

Wasteneys

2009

Cell Motil. Cytoskeleton

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“…The regulation of actin organization by plant myosins has been observed in many studies; however, the results vary in different cell types and based on different methods for inhibiting myosin activity. BDM inhibits the ATPase activity of myosin head domain (Funaki et al, 2004), and its effect on actin filaments in plant cells varies depending on the dose and duration of treatment. Treatment of pollen tubes and root hairs with BDM for 1 h causes a loss of longitudinal orientation of actin bundles in the shank region (Tominaga et al, 2000), whereas short-term treatment (10 min) of growing root hairs with BDM induces the formation of fine actin filament arrays extending into the apical clear zone (Zheng et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

“…A detailed description of the dynamic behavior of individual actin filaments in epidermal cells shows that BDM inhibits the turnover and shape change of actin filaments (Staiger et al, 2009). Although there is evidence that BDM can inhibit the motility of plant myosin XI in vitro (Tominaga et al, 2000;Funaki et al, 2004), this drug is typically applied at millimolar concentrations and probably does not inhibit all myosin-dependent cellular processes in plant cells (McCurdy, 1999). Therefore, genetic approaches using knockout mutants are important to interrogate the function of plant myosins.…”

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confidence: 99%

Arabidopsis Myosin XI: A Motor Rules the Tracks

et al. 2014

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Plant cell expansion relies on intracellular trafficking of vesicles and macromolecules, which requires myosin motors and a dynamic actin network. Arabidopsis (Arabidopsis thaliana) myosin XI powers the motility of diverse cellular organelles, including endoplasmic reticulum, Golgi, endomembrane vesicles, peroxisomes, and mitochondria. Several recent studies show that there are changes in actin organization and dynamics in myosin xi mutants, indicating that motors influence the molecular tracks they use for transport. However, the mechanism by which actin organization and dynamics are regulated by myosin XI awaits further detailed investigation. Here, using high spatiotemporal imaging of living cells, we quantitatively assessed the architecture and dynamic behavior of cortical actin arrays in a mutant with three Myosin XI (XI-1, XI-2, and XI-K) genes knocked out (xi3KO). In addition to apparent reduction of organ and cell size, the mutant showed less dense and more bundled actin filament arrays in epidermal cells. Furthermore, the overall actin dynamicity was significantly inhibited in the xi3KO mutant. Because cytoskeletal remodeling is contributed mainly by filament assembly/disassembly and translocation/buckling, we also examined the dynamic behavior of individual actin filaments. We found that the xi3KO mutant had significantly decreased actin turnover, with a 2-fold reduction in filament severing frequency. Moreover, quantitative analysis of filament shape change over time revealed that myosin XI generates the force for buckling and straightening of both single actin filaments and actin bundles. Thus, our data provide genetic evidence that three Arabidopsis class XI myosins contribute to actin remodeling by stimulating turnover and generating the force for filament shape change.

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“…The streaming of ER is impaired, and the morphology and organization of ER is altered in mutants of myosin XI, especially myosin XI-K, indicating this myosin XI isoform primary contributor to ER streaming, which is implicated intimately in the cytoplasmic streaming. An inhibitor of myosin activities, BDM (2,3-butanedione monoxime) that can suppress the motile activity in vitro of lily 170-kDa myosin XI [97] and Chara myosin XI [24], also completely suppresses such ER dynamics. These observations further indicate that the sliding movement of myosin XI is involved in maintaining ER morphology.…”

Section: Cytoplasmic Streaming In Higher Plant Cellsmentioning

confidence: 99%