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MBC in Press, published online ahead of print August 3, 2005
Mol. Biol. Cell 10.1091/mbc.E04-12-1114

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Submitted on December 23, 2004
Revised on July 21, 2005
Accepted on July 26, 2005

Role of Septins and the Exocyst Complex in the Function of Hydrolytic Enzymes Responsible for Fission Yeast Cell Separation

Ana Belén Martín-Cuadrado,* Jennifer L. Morrell,{dagger} Mami Konomi,{ddagger} Hanbing An,{dagger} Claudia Petit,{dagger} Masako Osumi,{ddagger} Mohan Balasubramanian,{sect} Kathleen L. Gould,{dagger} Francisco del Rey,* and Carlos R. Vázquez de Aldana*

*Instituto de Microbiología Bioquímica, Departamento de Microbiología y Genética, CSIC/ Universidad de Salamanca, 37007 Salamanca, Spain; {dagger}HHMI and Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37212; {ddagger}Laboratory of Electron Microscopy/Open Research Center, Japan Women’s University, Bunkyo-ku, Tokyo 112-8681, Japan; {sect}Laboratory of Cell Division, Temasek Life Sciences Laboratory, Singapore 117604, Singapore

Monitoring Editor: Anthony Bretscher

Cell separation in Schizosaccharomyces pombe is achieved by the concerted action of the Eng1 endo-{beta}-1,3-glucanase and the Agn1 endo-{alpha}-1,3-glucanase, which are transported to the septum and localize to a ring-like structure that surrounds the septum. The requirements for the correct localization of both hydrolases as a ring were analyzed using GFP fusion proteins. Targeting to the septum required a functional exocyst, since both proteins failed to localize correctly in sec8-1 or exo70{Delta} mutants, suggesting that Agn1 and Eng1 might be two of the cargo proteins present in the vesicles that accumulate in exocyst mutants. Septins and Mid2 were also required for correct formation of a ring. In their absence, Eng1 and Agn1 were found in a disk-like structure that spanned the septum, rather than in a ring. Even though septin and mid2{Delta} mutants have a cell separation defect, the septum and the distribution of linear {beta}-1,3-glucans were normal in these cells, suggesting that mislocalization of Eng1 and Agn1 might be the reason underlying the failure to separate efficiently. Thus, one of the functions of the septin ring would be to act as a positional marker for the localization of hydrolytic proteins to the medial region.

Address correspondence to: Carlos R. Vázquez de Aldana (cvazquez{at}usal.es)




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