ArticleMolecular biology of the cell2001
Identification of two type V myosins in fission yeast, one of which functions in polarized cell growth and moves rapidly in the cell.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 97 citations in OpenAlex.
- UCS Chaperone Folding of the Myosin Head: A Function That Evolved before Animals and Fungi Diverged from a Common Ancestor More than a Billion Years Ago.Biomolecules · 2022Review
- Involvement of Smi1 in cell wall integrity and glucan synthase Bgs4 localization during fission yeast cytokinesis.Molecular biology of the cell · 2022Article
- Review
- Microtubule-independent movement of the fission yeast nucleus.Journal of cell science · 2021Article
- Yeasts as Complementary Model Systems for the Study of the Pathological Repercussions of Enhanced Synphilin-1 Glycation and Oxidation.International journal of molecular sciences · 2021Article
- Temperature sensitive point mutations in fission yeast tropomyosin have long range effects on the stability and function of the actin-tropomyosin copolymer.Biochemical and biophysical research communications · 2018Article
- Active transport of cytoophidia in Schizosaccharomyces pombe.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Dependency relationships within the fission yeast polarity network.FEBS letters · 2018Article
- A class-II myosin is required for growth, conidiation, cell wall integrity and pathogenicity of Magnaporthe oryzae.Virulence · 2017Article
- A systematic screen for morphological abnormalities during fission yeast sexual reproduction identifies a mechanism of actin aster formation for cell fusion.PLoS genetics · 2017Article
- Analysis of biophysical and functional consequences of tropomyosin-fluorescent protein fusions.FEBS letters · 2016Article
- A single-headed fission yeast myosin V transports actin in a tropomyosin-dependent manner.The Journal of cell biology · 2016Article
- TOR complex 2 localises to the cytokinetic actomyosin ring and controls the fidelity of cytokinesis.Journal of cell science · 2016Article
- Microscopy of Fission Yeast Sexual Lifecycle.Journal of visualized experiments : JoVE · 2016Article
- Three myosins contribute uniquely to the assembly and constriction of the fission yeast cytokinetic contractile ring.Current biology : CB · 2015Article
- Evolutionarily conserved sites in yeast tropomyosin function in cell polarity, transport and contractile ring formation.Biology open · 2015Article
- A formin-nucleated actin aster concentrates cell wall hydrolases for cell fusion in fission yeast.The Journal of cell biology · 2015Article
- Fission yeast tropomyosin specifies directed transport of myosin-V along actin cables.Molecular biology of the cell · 2014Article
- In vitro contraction of cytokinetic ring depends on myosin II but not on actin dynamics.Nature cell biology · 2013Article
- Insight into actin organization and function in cytokinesis from analysis of fission yeast mutants.Genetics · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We characterized the novel Schizosaccharomyces pombe genes myo4(+) and myo5(+), both of which encode myosin-V heavy chains. Disruption of myo4 caused a defect in cell growth and led to an abnormal accumulation of secretory vesicles throughout the cytoplasm. The mutant cells were rounder than normal, although the sites for cell polarization were still established. Elongation of the cell ends and completion of septation required more time than in wild-type cells, indicating that Myo4 functions in polarized growth both at the cell ends and during septation. Consistent with this conclusion, Myo4 was localized around the growing cell ends, the medial F-actin ring, and the septum as a cluster of dot structures. In living cells, the dots of green fluorescent protein-tagged Myo4 moved rapidly around these regions. The localization and movement of Myo4 were dependent on both F-actin cables and its motor activity but seemed to be independent of microtubules. Moreover, the motor activity of Myo4 was essential for its function. These results suggest that Myo4 is involved in polarized cell growth by moving with a secretory vesicle along the F-actin cables around the sites for polarization. In contrast, the phenotype of myo5 null cells was indistinguishable from that of wild-type cells. This and other data suggest that Myo5 has a role distinct from that of Myo4.
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