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A more recent version of this article appeared on July 29, 2005
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M502660200v1
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Papers In Press, published online ahead of print May 27, 2005
J. Biol. Chem, 10.1074/jbc.M502660200
Submitted on March 10, 2005
Revised on May 27, 2005
Accepted on May 27, 2005

Phosphatidylinositol-4-phosphate-5-kinase regulates fission yeast cell integrity through a phospholipase C-mediated protein kinase C-independent pathway

Lu Deng, Reiko Sugiura, Kazuki Ohta, Kazuki Tada, Masahiro Suzuki, Masato Hirata, Shun-ichi Nakamura, Hisato Shuntoh, and Takayoshi Kuno

Department of Genome Sciences, Kobe University, Kobe 650-0017

Corresponding Author: tkuno{at}med.kobe-u.ac.jp

Fission yeast its3-1 mutant is an allele of the essential gene its3+ that encodes a phosphatidylinositol-4-phosphate-5-kinase (PIP5K) that produces phosphatidylinositol 4,5-bisphosphate (PIP2). We found that the its3-1 mutant is sensitive to micafungin, a (1,3)-beta-D-glucan synthase inhibitor, suggesting a cell wall integrity defect. Consistently, its3-1 mutation caused synthetic lethality with a (1,3)-beta-D-glucan synthase mutant, bgs1-i2, and its3-1 mutant cells showed aberrant localization of GFP-Bgs1. Similar aberrant localization of GFP-tagged Rgf1, a putative PIP2-binding guanine nucleotide exchange factor for Rho protein, in its3-1 mutants was observed, suggesting a defective Rgf1/Rho pathway. To unravel the molecular mechanism(s), putative downstream components of PIP5K signaling were analyzed. Unexpectedly, the overexpression of the phospholipase C (Plc1), but not that of protein kinase C (PKC, Pck1 and Pck2), suppressed the phenotypes of the its3-1 mutant. These findings indicate that PKCs are not involved in the suppression, and further analysis revealed that PKCs are not downstream of Plc1 in fission yeast. Also, the enzymatic activity of Plc1 is essential for the suppression of the phenotypes and for the viability of the its3-1 mutant. These findings suggest that Its3 PIP5K regulates cell integrity through a Plc1-mediated PKC-independent pathway, in addition to the Rho/PKC pathway.


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