ArticleEukaryotic cell2010
Schizosaccharomyces pombe calmodulin, Cam1, plays a crucial role in sporulation by recruiting and stabilizing the spindle pole body components responsible for assembly of the forespore membrane.
Article in Eukaryotic cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Effects ofCurrent issues in molecular biology · 2024Article
- Sporulation: A response to starvation in the fission yeast Schizosaccharomyces pombe.MicrobiologyOpen · 2022Review
- Acetylation stabilises calmodulin-regulated calcium signalling.FEBS letters · 2022Article
- Review
- Article
- The fission yeast SPB component Dms1 is required to initiate forespore membrane formation and maintain meiotic SPB components.PloS one · 2018Article
- Cell-surface copper transporters and superoxide dismutase 1 are essential for outgrowth during fungal spore germination.The Journal of biological chemistry · 2017Article
- The exocytic Rabs Ypt3 and Ypt2 regulate the early step of biogenesis of the spore plasma membrane in fission yeast.Molecular biology of the cell · 2016Article
- The fission yeast pleckstrin homology domain protein Spo7 is essential for initiation of forespore membrane assembly and spore morphogenesis.Molecular biology of the cell · 2011Article
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
Calmodulin in Schizosaccharomyces pombe is encoded by the cam1(+) gene, which is indispensable for both vegetative growth and sporulation. Here, we report how Cam1 functions in spore formation. We found that Cam1 preferentially localized to the spindle pole body (SPB) during meiosis and sporulation. Formation of the forespore membrane, a precursor of the plasma membrane in spores, was blocked in a missense cam1 mutant, which was viable but unable to sporulate. Three SPB proteins necessary for the onset of forespore membrane formation, Spo2, Spo13, and Spo15, were unable to localize to the SPB in the cam1 mutant although five core SPB components that were tested were present. Recruitment of Spo2 and Spo13 is known to require the presence of Spo15 in the SPB. Notably, Spo15 was unstable in the cam1 mutant, and as a result, SPB localization of Spo2 and Spo13 was lost. Overexpression of Spo15 partially alleviated the sporulation defect in the cam1 mutant. These results indicate that calmodulin plays an essential role in forespore membrane formation by stably maintaining Spo15, and thus Spo2 and Spo13, at the SPB in meiotic cells.
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