Microtubule‐associated coiled‐coil protein Ssm4 is involved in the meiotic development in fission yeast

Yamashita, Akira; Watanabe, Yoshinori; Yamamoto, Masayuki

doi:10.1046/j.1365-2443.1997.1100307.x

Cited by 29 publications

(38 citation statements)

References 45 publications

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“…Ssm4p is a microtubule-binding protein produced under nutrient starvation (Yamashita et al, 1997) and has a similar domain arrangement to Glued-type proteins ( Fig. 1), with a CAP-Gly domain at its N terminus followed by a coiled-coil stretch (Brunner and Nurse, 2000) (Fig.…”

Section: Ssm4p Is Essential For the Oscillatory Nuclear Movement Durimentioning

confidence: 99%

“…The ssm4∆ strain frequently generated aberrant asci carrying less than four spores (Yamashita et al, 1997) (Table 3). Disruption of the dynein heavy chain gene dhc1 caused similar abnormal sporulation (Yamamoto et al, 1999) (Table 3).…”

Section: Ssm4p Is Essential For the Oscillatory Nuclear Movement Durimentioning

confidence: 99%

“…Ssm4p is localised to the SPB, microtubules and the point where microtubule plus ends contact the cell cortex in meiotic cells We previously reported that Ssm4p colocalised with microtubules in both mitotic and meiotic cells when expressed ectopically (Yamashita et al, 1997). To examine localisation of Ssm4p under natural conditions, we tagged endogenously expressed Ssm4p with GFP.…”

Section: Ssm4p Interacts With the Dynein Complexmentioning

confidence: 99%

“…We previously identified the ssm4 gene, which encodes a coiled-coil protein carrying a CAP-Gly microtubule-binding domain (Yamashita et al, 1997). Ssm4p has a similar domain structure to Glued.…”

Section: Introductionmentioning

confidence: 99%

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The p150-Glued Ssm4p regulates microtubular dynamics and nuclear movement in fission yeast

Niccoli

Yamashita

Nurse

et al. 2004

Journal of Cell Science

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During vegetative growth of the fission yeastSchizosaccharomyces pombe, microtubules nucleate from multiple microtubule organising centres (MTOCs) close to the nucleus, polymerising until they reach the end of the cell and then shrinking back to the cell centre. In response to mating pheromone, S. pombe undergoes a morphological switch from a vegetative to a shmooing growth pattern. The switch in growth mode is paralleled by a switch in microtubular dynamics. Microtubules nucleate mostly from a single MTOC and pull on the ends of the cell to move the nucleus back and forth. This movement continues after cellular and nuclear fusion in the zygote and is important to ensure correct chromosome pairing, recombination and segregation during meiosis. Here we show that Ssm4p, a p150-Glued protein, is induced specifically in response to pheromone and is required for this nuclear movement. Ssm4p is associated with the cytoplasmic dynein complex and together with the CLIP-170 homologue Tip1p regulates dynein heavy chain localisation. We also show that Ssm4p collaborates with Tip1p in establishing the shmooing microtubular array.

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Section: Ssm4p Is Essential For the Oscillatory Nuclear Movement Durimentioning

confidence: 99%

Section: Ssm4p Is Essential For the Oscillatory Nuclear Movement Durimentioning

confidence: 99%

Section: Ssm4p Interacts With the Dynein Complexmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The p150-Glued Ssm4p regulates microtubular dynamics and nuclear movement in fission yeast

Niccoli

Yamashita

Nurse

et al. 2004

Journal of Cell Science

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“…Glued homolog Ssm4 is indispensable for dynein localization and function in the horse-tail nuclear movement (Fujita et al, 2010;Niccoli et al, 2004;Yamashita et al, 1997). However, how dynactin regulates the function of dynein remains unknown.…”

Section: Introductionmentioning

confidence: 99%

Dynactin and Num1 cooperate to establish the cortical anchoring of cytoplasmic dynein inS. pombe

Fujita

Yamashita

Yamamoto

2015

Journal of Cell Science

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Chromosome movement during meiosis is crucial for homologous pairing and meiotic recombination. During meiotic prophase in fission yeast, rapid nuclear migration is dependent on cytoplasmic dynein, which is anchored to the cell cortex and pulls microtubules, thereby driving nuclear migration. However, the precise mechanisms underlying dynein localization and activation remain unclear. Here, we identified three subunits of dynactin in fission yeast: Arp1, Mug5 and Jnm1 (also known as Mug1). These subunits transiently colocalized with dynein foci at the cell cortex and were essential for the cortical anchoring of dynein. Cortical factor Num1 (also known as Mcp5), which was also required for dynein anchoring, bound to dynein independently of dynactin. Whereas Num1 suppressed the sliding of dynein foci along the cortex, Arp1, Mug5 and Jnm1 were involved in the regulation of shrinkage and bundling of microtubules. From these data, we propose that dynein anchoring is established by cooperation of transient assembly of dynactin and function of Num1 at the cell cortex.

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Nuclear Movement Enforcing Chromosome Alignment in Fission Yeast—Meiosis Without Homolog Synapsis

Ding

Hiraoka

Recombination and Meiosis

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Pairing of homologous chromosomes is a prerequisite for meiotic recombination. In most eukaryotic organisms, a synaptonemal complex is formed between homologous chromosomes along their entire lengths to stabilize pairing. Asynaptic organisms in which the canonical synaptonemal complex is not formed are still able to pair homologous chromosomes in a different way. In the fission yeast Schizosaccharomyces pombe, telomere clustering and oscillatory nuclear movement persist for the entire meiotic prophase. This characteristic chromosome arrangement promotes pairing of homologous chromosomes and may compensate for the lack of homolog synapsis.Here we review recent progress in elucidating the dynamics of homologous pairing, as well as the molecular mechanisms involved in the regulation of telomere clustering and nuclear movement in S. pombe. AbbreviationsFISH fluorescence in situ hybridization GFP green fluorescent protein KASH Klarsicht-ANC1-SYNE1 homology domain LE linear elements SC synaptonemal complex SPB spindle-pole body SUN Sad1-UNC84 homology domain

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Microtubule‐associated coiled‐coil protein Ssm4 is involved in the meiotic development in fission yeast

Cited by 29 publications

References 45 publications

The p150-Glued Ssm4p regulates microtubular dynamics and nuclear movement in fission yeast

The p150-Glued Ssm4p regulates microtubular dynamics and nuclear movement in fission yeast

Dynactin and Num1 cooperate to establish the cortical anchoring of cytoplasmic dynein inS. pombe

Nuclear Movement Enforcing Chromosome Alignment in Fission Yeast—Meiosis Without Homolog Synapsis

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