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Nonmedially assembled F-actin cables incorporate into the actomyosin ring in fission yeast

MPG-Autoren
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Yu,  Haochen
Wedlich-Söldner, Roland / Cellular Dynamics and Cell Patterning, Max Planck Institute of Biochemistry, Max Planck Society;

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Wedlich-Söldner,  Roland
Wedlich-Söldner, Roland / Cellular Dynamics and Cell Patterning, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Huang, J., Huang, Y., Yu, H., Subramanian, D., Padmanabhan, A., Thadani, R., et al. (2012). Nonmedially assembled F-actin cables incorporate into the actomyosin ring in fission yeast. JOURNAL OF CELL BIOLOGY, 199(5), 831-847. doi:10.1083/jcb.201209044.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-000E-7A19-1
Zusammenfassung
In many eukaryotes, cytokinesis requires the assembly and constriction of an actomyosin-based contractile ring. Despite the central role of this ring in cytokinesis, the mechanism of F-actin assembly and accumulation in the ring is not fully understood. In this paper, we investigate the mechanism of F-actin assembly during cytokinesis in Schizosaccharomyces pombe using lifeact as a probe to monitor actin dynamics. Previous work has shown that F-actin in the actomyosin ring is assembled de novo at the division site. Surprisingly, we find that a significant fraction of F-actin in the ring was recruited from formin-Cdc12p nucleated long actin cables that were generated at multiple nonmedial locations and incorporated into the ring by a combination of myosin II and myosin V activities. Our results, together with findings in animal cells, suggest that de novo F-actin assembly at the division site and directed transport of F-actin cables assembled elsewhere can contribute to ring assembly.