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Architecture and dynamic remodelling of the septin cytoskeleton during the cell cycle

Author

Listed:
  • Katy Ong

    (University of Pennsylvania Perelman School of Medicine)

  • Carsten Wloka

    (University of Pennsylvania Perelman School of Medicine
    Institut für Biologie, Freie Universität Berlin)

  • Satoshi Okada

    (University of Pennsylvania Perelman School of Medicine
    Present address: Department of Medical Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka 812-8582, Japan)

  • Tatyana Svitkina

    (University of Pennsylvania)

  • Erfei Bi

    (University of Pennsylvania Perelman School of Medicine)

Abstract

Septins perform diverse functions through the formation of filaments and higher-order structures. However, the exact architecture of septin structures remains unclear. In the budding yeast Saccharomyces cerevisiae, septins form an ‘hourglass’ at the mother-bud neck before cytokinesis, which is converted into a ‘double ring’ during cytokinesis. Here, using platinum-replica electron microscopy, we find that the early hourglass consists of septin double filaments oriented along the mother-bud axis. In the late hourglass, these double filaments are connected by periodic circumferential single filaments on the membrane-proximal side and are associated with centrally located, circumferential, myosin-II thick filaments on the membrane-distal side. The double ring consists of exclusively circumferential septin filaments. Live-cell imaging studies indicate that the hourglass-to-double ring transition is accompanied by loss of septin subunits from the hourglass and reorganization of the remaining subunits into the double ring. This work provides an unparalleled view of septin structures within cells and defines their remodelling dynamics during the cell cycle.

Suggested Citation

  • Katy Ong & Carsten Wloka & Satoshi Okada & Tatyana Svitkina & Erfei Bi, 2014. "Architecture and dynamic remodelling of the septin cytoskeleton during the cell cycle," Nature Communications, Nature, vol. 5(1), pages 1-10, December.
  • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6698
    DOI: 10.1038/ncomms6698
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    Cited by:

    1. Maritzaida Varela Salgado & Ingrid E. Adriaans & Sandra A. Touati & Sandy Ibanes & Joséphine Lai-Kee-Him & Aurélie Ancelin & Luca Cipelletti & Laura Picas & Simonetta Piatti, 2024. "Phosphorylation of the F-BAR protein Hof1 drives septin ring splitting in budding yeast," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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