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Structural insights into yeast septin organization from polarized fluorescence microscopy

Author

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  • Alina M. Vrabioiu

    (Harvard Medical School)

  • Timothy J. Mitchison

    (Harvard Medical School)

Abstract

Hourglass figures There are few analytical methods available for solving cellular structure in the important sub-micrometre range. Alina Vrabioiu and Timothy Mitchison have developed a new one, and used it to resolve a long-standing controversy about the structure of the 'hourglass' feature in dividing yeast cells. Polarized fluorescence microscopy of rigidly attached GFP was used to determine septin filament organization and the dynamics of septin, a polymerizing GTPase intimately involved in cell division. The filaments are seen to form ordered assemblies in living yeast and undergo a 90° rotation before the onset of cytokinesis.

Suggested Citation

  • Alina M. Vrabioiu & Timothy J. Mitchison, 2006. "Structural insights into yeast septin organization from polarized fluorescence microscopy," Nature, Nature, vol. 443(7110), pages 466-469, September.
    • Handle: RePEc:nat:nature:v:443:y:2006:i:7110:d:10.1038_nature05109
    DOI: 10.1038/nature05109
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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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