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Open Life Sciences

formerly Central European Journal of Biology

Editor-in-Chief: Ratajczak, Mariusz

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Volume 4, Issue 3 (Sep 2009)

Issues

Fungal septins: one ring to rule it all?

Alberto González-Novo
  • Department of Microbiology and Genetics, Institute of Microbiology and Biochemistry, Salamanca University/CSIC, 37007, Salamanca, Spain
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/ Carlos Vázquez de Aldana
  • Department of Microbiology and Genetics, Institute of Microbiology and Biochemistry, Salamanca University/CSIC, 37007, Salamanca, Spain
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/ Javier Jiménez
  • Cell Signalling Unit, Department of Health and Experimental Sciences, Pompeu Fabra University, 08003, Barcelona, Spain
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Published Online: 2009-07-26 | DOI: https://doi.org/10.2478/s11535-009-0032-2

Abstract

Septins are a conserved family of GTP-binding proteins found in living organisms ranging from yeasts to mammals. They are able to polymerize and form hetero-oligomers that assemble into higher-order structures whose detailed molecular architecture has recently been described in different organisms. In Saccharomyces cerevisiae, septins exert numerous functions throughout the cell cycle, serving as scaffolds for many different proteins or as diffusion barriers at the bud neck. In other fungi, septins are required for the proper completion of diverse functions such as polarized growth or pathogenesis. Recent results from several fungi have revealed important differences in septin organization and regulation as compared with S. cerevisiae, especially during Candida albicans hyphal growth and in Ashbya gossypii. Here we focus on these recent findings, their relevance in the biology of these eukaryotes and in consequence the “renaissance” of the study of septin structures in cells showing a different kind of morphological behaviour.

Keywords: Septins; Candida albicans; Saccharomyces cerevisiae; Morphogenesis; Filamentous fungi

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About the article

Published Online: 2009-07-26

Published in Print: 2009-09-01


Citation Information: Open Life Sciences, ISSN (Online) 2391-5412, DOI: https://doi.org/10.2478/s11535-009-0032-2.

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