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Originally published as MBC in Press, 10.1091/mbc.E07-09-0876 on January 30, 2008

Vol. 19, Issue 4, 1509-1518, April 2008

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Sep7 Is Essential to Modify Septin Ring Dynamics and Inhibit Cell Separation during Candida albicans Hyphal Growth

Alberto González-Novo*, Jaime Correa-Bordes{dagger}, Leticia Labrador*, Miguel Sánchez*, Carlos R. Vázquez de Aldana*, and Javier Jiménez*,{ddagger}

*Departmento Microbiología y Genética, Instituto de Microbiología Bioquímica, Universidad de Salamanca/Consejo Superior de Investigaciones Científicas, 37007 Salamanca, Spain; and {dagger}Departmento Ciencias Biomédicas, Facultad de Ciencias, Universidad de Extremadura, 06071 Badajoz, Spain

Submitted September 7, 2007; Revised January 14, 2008; Accepted January 23, 2008
Monitoring Editor: Daniel Lew

When Candida albicans yeast cells receive the appropriate stimulus, they switch to hyphal growth, characterized by continuous apical elongation and the inhibition of cell separation. The molecular basis of this inhibition is poorly known, despite its crucial importance for hyphal development. In C. albicans, septins are important for hypha formation and virulence. Here, we used fluorescence recovery after photobleaching analysis to characterize the dynamics of septin rings during yeast and hyphal growth. On hyphal induction, septin rings are converted to a hyphal-specific state, characterized by the presence of a frozen core formed by Sep7/Shs1, Cdc3 and Cdc12, whereas Cdc10 is highly dynamic and oscillates between the ring and the cytoplasm. Conversion of septin rings to the hyphal-specific state inhibits the translocation of Cdc14 phosphatase, which controls cell separation, to the hyphal septum. Modification of septin ring dynamics during hyphal growth is dependent on Sep7 and the hyphal-specific cyclin Hgc1, which partially controls Sep7 phosphorylation status and protein levels. Our results reveal a link between the cell cycle machinery and septin cytoskeleton dynamics, which inhibits cell separation in the filaments and is essential for hyphal morphogenesis.


This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/10.1091/mbc.E07-09-0876) on January 30, 2008.

{ddagger} Present address: Cell Signaling Unit, Departament de Cìences Experimentals i de la Salut, Universitat Pompeu Fabra, Dr. Aiguader 88, 08003 Barcelona, Spain.

Address correspondence to: Carlos R. Vázquez de Aldana (cvazquez{at}usal.es) or Javier Jiménez (javier.jimenezj{at}upf.edu).







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