Fission yeast Myo51 is a meiotic spindle pole body component with discrete roles during cell fusion and spore formation

Doyle, Alex; Martin-Garcia, Rebecca; Coulton, Arthur T.; Bagley, Steven; Mulvihill, Daniel P.

doi:10.1242/jcs.055202

Cited by 25 publications

(27 citation statements)

References 62 publications

(66 reference statements)

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“…However, the expression of each actin polymer labelling fusion protein we tested (i.e. GFP-CHD Rng2 , GFP-Cdc8, For3-GFP) (Doyle et al, 2009;Karagiannis et al, 2005;Martin and Chang, 2006;Skoumpla et al, 2007) rescued the naa25 strain cytokinenetic phenotypes (not shown). This not only indicates that each GFP fusion protein stabilises actin filaments and affects normal actin polymer dynamics, but suggests that the naa25 defect is brought about by instability of the actin ring.…”

Section: Resultsmentioning

confidence: 94%

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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Section: Resultsmentioning

confidence: 94%

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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“…1E; Dudin et al 2015). Fourth, the second type V myosin Myo51, which accumulates at the fusion focus late in the process (Doyle et al 2009;Dudin et al 2015), was detected in both cells only in committed pairs (Supplemental Fig. S1).…”

Section: A Diffusible Signal Is Necessary For Cell Fusionmentioning

confidence: 94%

Spatial focalization of pheromone/MAPK signaling triggers commitment to cell–cell fusion

2016

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Cell fusion is universal in eukaryotes for fertilization and development, but what signals this process is unknown. Here, we show in Schizosaccharomyces pombe that fusion does not require a dedicated signal but is triggered by spatial focalization of the same pheromone-GPCR (G-protein-coupled receptor)-MAPK signaling cascade that drives earlier mating events. Autocrine cells expressing the receptor for their own pheromone trigger fusion attempts independently of cell-cell contact by concentrating pheromone release at the fusion focus, a dynamic actin aster underlying the secretion of cell wall hydrolases. Pheromone receptor and MAPK cascade are similarly enriched at the fusion focus, concomitant with fusion commitment in wild-type mating pairs. This focalization promotes cell fusion by immobilizing the fusion focus, thus driving local cell wall dissolution. We propose that fusion commitment is imposed by a local increase in MAPK concentration at the fusion focus, driven by a positive feedback between fusion focus formation and focalization of pheromone release and perception.

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“…After agglutination, the cross wall separating both parental cells is degraded, allowing cell fusion. Efficient cell fusion requires the correct organization of the cytoskeleton (Petersen et al 1995(Petersen et al , 1998aKurahashi et al 2002;Doyle et al 2009). The S. cerevisiae FUS1 and the S. pombe fus1 + genes have the same name and both mutants exhibit cell fusion defects during mating, leading to an accumulation of prezygotes (mating intermediates in which the mating partners have established a stable contact but have not yet fused).…”

mentioning

confidence: 99%

Membrane Organization and Cell Fusion During Mating in Fission Yeast Requires Multipass Membrane Protein Prm1

et al. 2014

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The involvement of Schizosaccharomyces pombe prm1 + in cell fusion during mating and its relationship with other genes required for this process have been addressed. S. pombe prm1D mutant exhibits an almost complete blockade in cell fusion and an abnormal distribution of the plasma membrane and cell wall in the area of cell-cell interaction. The distribution of cellular envelopes is similar to that described for mutants devoid of the Fig1-related claudin-like Dni proteins; however, prm1 + and the dni + genes act in different subpathways. Time-lapse analyses show that in the wild-type S. pombe strain, the distribution of phosphatidylserine in the cytoplasmic leaflet of the plasma membrane undergoes some modification before an opening is observed in the cross wall at the cellcell contact region. In the prm1D mutant, this membrane modification does not take place, and the cross wall between the mating partners is not extensively degraded; plasma membrane forms invaginations and fingers that sometimes collapse/retract and that are sometimes strengthened by the synthesis of cell-wall material. Neither prm1D nor prm1D dniD zygotes lyse after cell-cell contact in medium containing and lacking calcium. Response to drugs that inhibit lipid synthesis or interfere with lipids is different in wild-type, prm1D, and dni1D strains, suggesting that membrane structure/organization/dynamics is different in all these strains and that Prm1p and the Dni proteins exert some functions required to guarantee correct membrane organization that are critical for cell fusion. M EMBRANE fusion is essential for several developmental processes. The characterization of mating in yeasts represents a useful tool for understanding the mechanisms involved in intercellular membrane merger and their regulation. In the fission yeast Schizosaccharomyces pombe, heterothallic cells belong to one of two mating types, M (h 2 cells) or P (h + cells) while h 90 strains are homothallic (Arcangioli and Thon 2004). In rich medium, h + and h 2 cells can proliferate actively together without mating. When nitrogen becomes scarce the cAMP level decreases, which triggers the expression of genes required for sexual differentiation. Cells arrest in G1 and polarize, giving rise to specialized cells termed shmoos (Yamamoto et al. 1997;Davey 1998;Nielsen 2004;Yamamoto 2004). After agglutination, the cross wall separating both parental cells is degraded, allowing cell fusion. Efficient cell fusion requires the correct organization of the cytoskeleton (Petersen et al. 1995(Petersen et al. , 1998aKurahashi et al. 2002;Doyle et al. 2009). The S. cerevisiae FUS1 and the S. pombe fus1 + genes have the same name and both mutants exhibit cell fusion defects during mating, leading to an accumulation of prezygotes (mating intermediates in which the mating partners have established a stable contact but have not yet fused). However, the corresponding proteins are not related; while Saccharomyces cerevisiae Fus1p is a membrane protein (Trueheart et al. 1987), S. pombe Fus1p ...

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Fission yeast Myo51 is a meiotic spindle pole body component with discrete roles during cell fusion and spore formation

Cited by 25 publications

References 62 publications

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

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

Spatial focalization of pheromone/MAPK signaling triggers commitment to cell–cell fusion

Membrane Organization and Cell Fusion During Mating in Fission Yeast Requires Multipass Membrane Protein Prm1

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