In vivo movement of the type V myosin Myo52 requires dimerisation but is independent of the neck domain

Grallert, Ágnes; Martin-Garcia, Rebecca; Bagley, Steven; Mulvihill, Daniel P.

doi:10.1242/jcs.012468

Cited by 20 publications

(26 citation statements)

References 27 publications

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“…This simple approach supports the ultimate controlled experiment: the simultaneous imaging of two genetically distinct cells in the same field of view, where one culture is labeled with a fluorescent lectin whereas the other is not ( Fig. 1B; Beinhauer et al 1997;Alvarez-Tabarés et al 2007;Grallert et al 2007;Attanapola 2009;Martín-García and Mulvihill 2009). Alternatively, an additional fusion protein at a distinct location that emits at a different wavelength can be incorporated into the control strain (Fig.…”

Section: Mountingsupporting

confidence: 59%

Live Cell Imaging in Fission Yeast

Mulvihill

2017

Cold Spring Harb Protoc

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Live cell imaging complements the array of biochemical and molecular genetic approaches to provide a comprehensive insight into functional dependencies and molecular interactions in fission yeast. Fluorescent proteins and vital dyes reveal dynamic changes in the spatial distribution of organelles and the proteome and how each alters in response to changes in environmental and genetic composition. This introduction discusses key issues and basic image analysis for live cell imaging of fission yeast.

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Section: Mountingsupporting

confidence: 59%

Live Cell Imaging in Fission Yeast

Mulvihill

2017

Cold Spring Harb Protoc

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“…Live-cell imaging confirmed that Myo52 made frequent long-distance cytoplasmic movements and concentrated to non-motile foci at the growing cell tips (Fig. 1B) (Grallert et al, 2007). By contrast, Myo52-1 failed to concentrate to the actin-patch-rich cell tips to the same extent as the wild-type protein and made relatively short and less frequent excursions within the cell (Fig.…”

Section: Motor Activity Of Myosin V Regulates Microtubule Catastrophementioning

confidence: 73%

Myosin V spatially regulates microtubule dynamics and promotes the ubiquitin-dependent degradation of the fission yeast CLIP-170 homologue, Tip1

Martín‐García

Mulvihill

2009

Journal of Cell Science

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Coordination between microtubule and actin cytoskeletons plays a crucial role during the establishment of cell polarity. In fission yeast, the microtubule cytoskeleton regulates the distribution of actin assembly at the new growing end during the monopolar-to-bipolar growth transition. Here, we describe a novel mechanism in which a myosin V modulates the spatial coordination of proteolysis and microtubule dynamics. In cells lacking a functional copy of the class V myosin, Myo52, the plus ends of microtubules fail to undergo catastrophe on contacting the cell end and continue to grow, curling around the end of the cell. We show that this actin-associated motor regulates the efficient ubiquitin-dependent proteolysis of the Schizosaccharomyces pombe CLIP-170 homologue, Tip1. Myo52 facilitates microtubule catastrophe by enhancing Tip1 removal from the plus end of growing microtubules at the cell tips. There, Myo52 and the ubiquitin receptor, Dph1, work in concert to target Tip1 for degradation. Supplementary material available online at

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“…Myo52 moves along Cdc8-actin polymers within the S. pombe cell and concentrates at actin-rich sites of cell growth (Grallert et al, 2007). Not only was the ability of Myo52 to localise to actin filaments or concentrate at regions of growth unaffected in the naa25 cells (Fig.…”

Section: Cellular Distribution and Dynamics Of Class I And V Myosin Amentioning

confidence: 93%

The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast

Coulton

East

Galinska-Rakoczy

et al. 2010

Journal of Cell Science

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SummaryTropomyosin (Tm) is a conserved dimeric coiled-coil protein, which forms polymers that curl around actin filaments in order to regulate actomyosin function. Acetylation of the Tm N-terminal methionine strengthens end-to-end bonds, which enhances actin binding as well as the ability of Tm to regulate myosin motor activity in both muscle and non-muscle cells. In this study we explore the function of each Tm form within fission yeast cells. Electron microscopy and live cell imaging revealed that acetylated and unacetylated Tm associate with distinct actin structures within the cell, and that each form has a profound effect upon the shape and integrity of the polymeric actin filament. We show that, whereas Tm acetylation is required to regulate the in vivo motility of class II myosins, acetylated Tm had no effect on the motility of class I and V myosins. These findings illustrate a novel Tm-acetylation-statedependent mechanism for regulating specific actomyosin cytoskeletal interactions.

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In vivo movement of the type V myosin Myo52 requires dimerisation but is independent of the neck domain

Abstract: SummaryIn vivo movement of the type V myosin Myo52 requires dimerisation but is independent of the neck domain

Cited by 20 publications

References 27 publications

Live Cell Imaging in Fission Yeast

Live Cell Imaging in Fission Yeast

Myosin V spatially regulates microtubule dynamics and promotes the ubiquitin-dependent degradation of the fission yeast CLIP-170 homologue, Tip1

The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast

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