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Originally published as MBC in Press, 10.1091/mbc.E04-12-1114 on August 3, 2005

Vol. 16, Issue 10, 4867-4881, October 2005

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

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

* Instituto de Microbiología Bioquímica, Departamento de Microbiología y Genética, Consejo Superior de Investigaciones Cientificas/Universidad de Salamanca, 37007 Salamanca, Spain; {dagger} Howard Hughes Medical Institute 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; and § Laboratory of Cell Division, Temasek Life Sciences Laboratory, Singapore 117604, Singapore

Submitted December 23, 2004; Revised July 21, 2005; Accepted July 26, 2005
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 ringlike structure that surrounds the septum. The requirements for the correct localization of both hydrolases as a ring were analyzed using green fluorescent protein fusion proteins. Targeting to the septum required a functional exocyst, because 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 disklike 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.


This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E04-12-1114) on August 3, 2005.

Abbreviations used: CAR, contractile actomyosin ring.

{boxv} The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

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




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