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Originally published as MBC in Press, 10.1091/mbc.E08-05-0479 on September 17, 2008

Vol. 19, Issue 12, 5214-5225, December 2008

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The Sur7 Protein Regulates Plasma Membrane Organization and Prevents Intracellular Cell Wall Growth in Candida albicans

Francisco J. Alvarez*, Lois M. Douglas, Adam Rosebrock, and James B. Konopka

Department of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, NY 11794-5222

Submitted May 14, 2008; Revised August 29, 2008; Accepted September 10, 2008
Monitoring Editor: Daniel J. Lew

The Candida albicans plasma membrane plays important roles in cell growth and as a target for antifungal drugs. Analysis of Ca-Sur7 showed that this four transmembrane domain protein localized to stable punctate patches, similar to the plasma membrane subdomains known as eisosomes or MCC that were discovered in S. cerevisiae. The localization of Ca-Sur7 depended on sphingolipid synthesis. In contrast to S. cerevisiae, a C. albicans sur7{Delta} mutant displayed defects in endocytosis and morphogenesis. Septins and actin were mislocalized, and cell wall synthesis was very abnormal, including long projections of cell wall into the cytoplasm. Several phenotypes of the sur7{Delta} mutant are similar to the effects of inhibiting β-glucan synthase, suggesting that the abnormal cell wall synthesis is related to activation of chitin synthase activity seen under stress conditions. These results expand the roles of eisosomes by demonstrating that Sur7 is needed for proper plasma membrane organization and cell wall synthesis. A conserved Cys motif in the first extracellular loop of fungal Sur7 proteins is similar to a characteristic motif of the claudin proteins that form tight junctions in animal cells, suggesting a common role for these tetraspanning membrane proteins in forming specialized plasma membrane domains.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E08-05-0479) on September 17, 2008.

* Present address: Department of Cell Biology, Wenner-Gren Institute, Stockholm University, SE-106 91 Stockholm, Sweden.

Address correspondence to: James B. Konopka (james.konopka{at}sunysb.edu)

Abbreviations used: MCC, membrane compartment occupied by Can1; TMD, transmembrane domain.




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