Plant Myosins

Yokota, Etsuo; Shimmen, Teruo

doi:10.1007/978-1-4419-0987-9_2

Cited by 4 publications

(2 citation statements)

References 126 publications

(226 reference statements)

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“…7). Myosin XI is believed to be associated with its targeting organelles and vesicles through its C-terminal tail region, with the expressed tail region of myosin XI in living cells exerting dominantly strong negative effects on the movement and transport of organelles such as Golgi, mitochondria, and peroxisomes (Yokota and Shimmen, 2011). Consistent with this observation, the recombinant protein containing the C-terminal tail region of 175-kD myosin dissociated this myosin from microsomes (Supplemental Fig.…”

Section: The Movement Of Myosin XI Responsible For Er Tubule Formationsupporting

confidence: 64%

Myosin XI-Dependent Formation of Tubular Structures from Endoplasmic Reticulum Isolated from Tobacco Cultured BY-2 Cells

Yokota

Ueda²,

Hashimoto³

et al. 2011

Plant Physiology

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The reticular network of the endoplasmic reticulum (ER) consists of tubular and lamellar elements and is arranged in the cortical region of plant cells. This network constantly shows shape change and remodeling motion. Tubular ER structures were formed when GTP was added to the ER vesicles isolated from tobacco (Nicotiana tabacum) cultured BY-2 cells expressing ER-localized green fluorescent protein. The hydrolysis of GTP during ER tubule formation was higher than that under conditions in which ER tubule formation was not induced. Furthermore, a shearing force, such as the flow of liquid, was needed for the elongation/ extension of the ER tubule. The shearing force was assumed to correspond to the force generated by the actomyosin system in vivo. To confirm this hypothesis, the S12 fraction was prepared, which contained both cytosol and microsome fractions, including two classes of myosins, XI (175-kD myosin) and VIII (BY-2 myosin VIII-1), and ER-localized green fluorescent protein vesicles. The ER tubules and their mesh-like structures were arranged in the S12 fraction efficiently by the addition of ATP, GTP, and exogenous filamentous actin. The tubule formation was significantly inhibited by the depletion of 175-kD myosin from the S12 fraction but not BY-2 myosin VIII-1. Furthermore, a recombinant carboxyl-terminal tail region of 175-kD myosin also suppressed ER tubule formation. The tips of tubules moved along filamentous actin during tubule elongation. These results indicated that the motive force generated by the actomyosin system contributes to the formation of ER tubules, suggesting that myosin XI is responsible not only for the transport of ER in cytoplasm but also for the reticular organization of cortical ER.

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Section: The Movement Of Myosin XI Responsible For Er Tubule Formationsupporting

confidence: 64%

Myosin XI-Dependent Formation of Tubular Structures from Endoplasmic Reticulum Isolated from Tobacco Cultured BY-2 Cells

Yokota

Ueda²,

Hashimoto³

et al. 2011

Plant Physiology

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“…Myosins are mechanochemical enzymes with actin-activated ATPase activity in the conserved head domain; evolutionarily, plant myosins belong to classes VIII and XI in the superfamily of eukaryotic myosins (99,111,128). Through cargo-binding domains in the tail, myosins power the movement of a diverse array of organelles and membrane-bound vesicles along actin filament cables.…”

Section: Actin-binding Proteins Regulate Filament Array Architecture mentioning

confidence: 99%

Signaling to Actin Stochastic Dynamics

Li¹,

Blanchoin

Staiger

2015

Annu. Rev. Plant Biol.

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Advances in microscopy techniques applied to living cells have dramatically transformed our view of the actin cytoskeleton as a framework for cellular processes. Conventional fluorescence imaging and static analyses are useful for quantifying cellular architecture and the network of filaments that support vesicle trafficking, organelle movement, and response to biotic stress. However, new imaging techniques have revealed remarkably dynamic features of individual actin filaments and the mechanisms that underpin their construction and turnover. In this review, we briefly summarize knowledge about actin and actin-binding proteins in plant systems. We focus on the quantitative properties of the turnover of individual actin filaments, highlight actin-binding proteins that participate in actin dynamics, and summarize the current genetic evidence that has been used to dissect specific aspects of the stochastic dynamics model. Finally, we describe some signaling pathways in which recent data implicate changes in actin filament dynamics and the associated cytoplasmic responses.

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