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Eukaryotic Cell, July 2009, p. 1027-1037, Vol. 8, No. 7
1535-9778/09/$08.00+0     doi:10.1128/EC.00095-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Protein Phosphatase Type 1-Interacting Protein Ysw1 Is Involved in Proper Septin Organization and Prospore Membrane Formation during Sporulation ^,

Makoto Ishihara,^1, Yasuyuki Suda,^2,, Ichiro Inoue,¹ Takayuki Tanaka,¹ Tetsuo Takahashi,³ Xiao-Dong Gao,⁴ Yasuhisa Fukui,^1,|| Sayoko Ihara,¹ Aaron M. Neiman,² and Hiroyuki Tachikawa^1*

Laboratory of Biological Chemistry, Graduate School of Agricultural and Life Science, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan,¹ Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 11794-5215,² Department of Applied Biochemistry, School of Engineering, Tokai University, Kitakaname 1117, Hiratsuka, Kanagawa 259-1292, Japan,³ Graduate School of Advanced Life Science, Frontier Research Center for Post-Genomic Science and Technology, Hokkaido University, N21, W11, Kita-Ku, Sapporo 001-0021, Japan⁴

Received 26 March 2009/ Accepted 11 May 2009

Sporulation of Saccharomyces cerevisiae is a developmental process in which four haploid spores are generated inside a diploid cell. Gip1, a sporulation-specific targeting subunit of protein phosphatase type 1, together with its catalytic subunit, Glc7, colocalizes with septins along the extending prospore membrane and is required for septin organization and spore wall formation. However, the mechanism by which Gip1-Glc7 phosphatase promotes these events is unclear. We show here that Ysw1, a sporulation-specific coiled-coil protein, has a functional relationship to Gip1-Glc7 phosphatase. Overexpression of YSW1 partially suppresses the sporulation defect of a temperature-sensitive allele of gip1. Ysw1 interacts with Gip1 in a two-hybrid assay, and this interaction is required for suppression. Ysw1 tagged with green fluorescent protein colocalizes with septins and Gip1 along the extending prospore membrane during spore formation. Sporulation is partially defective in ysw1 mutant, and cytological analysis revealed that septin structures are perturbed and prospore membrane extension is aberrant in ysw1 cells. These results suggest that Ysw1 functions with the Gip1-Glc7 phosphatase to promote proper septin organization and prospore membrane formation.

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* Corresponding author. Mailing address: Laboratory of Biological Chemistry, Graduate School of Agriculture and Life Science, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan. Phone: 81-3-5841-5113. Fax: 81-3-5841-8024. E-mail: atachi{at}mail.ecc.u-tokyo.ac.jp

Published ahead of print on 22 May 2009.

Supplemental material for this article may be found at http://ec.asm.org/.

M.I. and Y.S. contributed equally to this study.

Present address: Molecular Membrane Biology Laboratory, Riken Advanced Science Institute, Wako, Saitama 351-0198, Japan.

^|| Present address: Laboratory of Cell Biology, Hoshi University, 2-4-1 Ebara, Shinagawa-ku, Tokyo 142-8501, Japan.

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Eukaryotic Cell, July 2009, p. 1027-1037, Vol. 8, No. 7
1535-9778/09/$08.00+0     doi:10.1128/EC.00095-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.