Papers - TAKEDA Kojiro
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Phosphate uptake restriction, phosphate export, and polyphosphate synthesis contribute synergistically to cellular proliferation and survival. Reviewed International journal
Masahiro Takado, Tochi Komamura, Tomoki Nishimura, Ikkei Ohkubo, Keita Ohuchi, Tomohiro Matsumoto, Kojiro Takeda
The Journal of biological chemistry 299 ( 12 ) 105454 - 105454 2023.11
Authorship：Last author, Corresponding author
Phosphate (Pi) is a macronutrient, and Pi homeostasis is essential for life. Pi homeostasis has been intensively studied; however, many questions remain, even at the cellular level. Using Schizosaccharomyces pombe, we sought to better understand cellular Pi homeostasis and showed that three Pi regulators with SPX domains, Xpr1/Spx2, Pqr1, and the VTC complex synergistically contribute to Pi homeostasis to support cell proliferation and survival. SPX domains bind to inositol pyrophosphate and modulate activities of Pi-related proteins. Xpr1 is a plasma membrane protein and its Pi-exporting activity has been demonstrated in metazoan orthologs, but not in fungi. We first found that S. pombe Xpr1 is a Pi exporter, activity of which is regulated and accelerated in the mutants of Pqr1 and the VTC complex. Pqr1 is the ubiquitin ligase downregulating the Pi importers, Pho84 and Pho842. The VTC complex synthesizes polyphosphate in vacuoles. Triple deletion of Xpr1, Pqr1, and Vtc4, the catalytic core of the VTC complex, was nearly lethal in normal medium but survivable at lower [Pi]. All double-deletion mutants of the three genes were viable at normal Pi, but Δpqr1Δxpr1 showed severe viability loss at high [Pi], accompanied by hyper-elevation of cellular total Pi and free Pi. This study suggests that the three cellular processes, restriction of Pi uptake, Pi export, and polyP synthesis, contribute synergistically to cell proliferation through maintenance of Pi homeostasis, leading to the hypothesis that cooperation between Pqr1, Xpr1, and the VTC complex protects the cytoplasm and/or the nucleus from lethal elevation of free Pi.
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Regulation of inorganic polyphosphate is required for proper vacuolar proteolysis in fission yeast. Reviewed International journal
Naoya Sawada, Shiori Ueno, Kojiro Takeda
The Journal of biological chemistry 297 ( 1 ) 100891 - 100891 2021.7
Regulation of cellular proliferation and quiescence is a central issue in biology that has been studied using model unicellular eukaryotes, such as the fission yeast Schizosaccharomyces pombe. We previously reported that the ubiquitin/proteasome pathway and autophagy are essential to maintain quiescence induced by nitrogen deprivation in S. pombe; however, specific ubiquitin ligases that maintain quiescence are not fully understood. Here we investigated the SPX-RING-type ubiquitin ligase Pqr1, identified as required for quiescence in a genetic screen. Pqr1 is found to be crucial for vacuolar proteolysis, the final step of autophagy, through proper regulation of phosphate and its polymer polyphosphate. Pqr1 restricts phosphate uptake into the cell through ubiquitination and subsequent degradation of phosphate transporters on plasma membranes. We hypothesized that Pqr1 may act as the central regulator for phosphate control in S. pombe, through the function of the SPX domain involved in phosphate sensing. Deletion of pqr1+ resulted in hyperaccumulation of intracellular phosphate and polyphosphate and in improper autophagy-dependent proteolysis under conditions of nitrogen starvation. Polyphosphate hyperaccumulation in pqr1+-deficient cells was mediated by the polyphosphate synthase VTC complex in vacuoles. Simultaneous deletion of VTC complex subunits rescued Pqr1 mutant phenotypes, including defects in proteolysis and loss of viability during quiescence. We conclude that excess polyphosphate may interfere with proteolysis in vacuoles by mechanisms that as yet remain unknown. The present results demonstrate a connection between polyphosphate metabolism and vacuolar functions for proper autophagy-dependent proteolysis, and we propose that polyphosphate homeostasis contributes to maintenance of cellular viability during quiescence.
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The fission yeast Greatwall-Endosulfine pathway is required for proper quiescence/G<sub>0</sub> phase entry and maintenance. Reviewed
Aono S, Haruna Y, Watanabe YH, Mochida S, Takeda K
Genes to Cells 24 ( 2 ) 172 - 186 2019.2
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Glucose restriction induces transient G2 cell cycle arrest extending cellular chronological lifespan Reviewed
Masuda, F., Ishii, M., Mori, A., Uehara, L., Yanagida, M., *Takeda, K., and *Saitoh, S. (*: corresponding author)
Sci Rep 6 19629 2016.1
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The critical glucose concentration for respiration-independent proliferation of fission yeast, Schizosaccharomyces pombe. Reviewed
*Takeda K, Starzynski C, Mori A, Yanagida M (* corresponding author)
Mitochondrion 22 91 - 95 2015.5
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The 19S proteasome subunit Rpt3 regulates distribution of CENP-A by associating with centromeric chromatin Reviewed
Kitagawa, T., Ishii, K., Takeda, K., and Matumoto, T.
Nature Communications 5 3597 2014.4
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Identification of genes affecting the toxicity of anti-cancer drug Bortezomib by genome-wide screening in S.pombe Reviewed
Takeda, K., Mori, A., and Yanagida, M.
PLoS One 7 ( 6 ) 2011
Joint Work
Authorship：Lead author, Corresponding author
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Nutrient Signaling via the TORC1-Greatwall-PP2A<sup>B55δ</sup> Pathway Responsible for the High Initial Rates of Alcoholic Fermentation in Sake Yeast Strains of <i>Saccharomyces cerevisiae</i>. Reviewed
Watanabe D, Kajihara T, Sugimoto Y, Takagi K, Mizuno M, Zhou Y, Chen J, Takeda K, Tatebe H, Shiozaki K, Nakazawa N, Izawa S, Akao T, Shimoi H, Maeda T, Takagi H
Applied and environmental microbiology 2018.10
Joint Work
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Diverse fission yeast genes required for responding to oxidative and metal stress: Comparative analysis of glutathione-related and other defense gene deletions.
Pluskal, T., Sajiki, K., Becker, J., Takeda, K., and Yanagida, M.
Genes Cells 21 ( 6 ) 530 - 542 2016.6
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Determination of D-Serine in several model organisms used for metabolic, developmental and/or genetic researches by liquid chromatogrphy/fluoresce detection and tandem mass spectrometry
Syuto, M., Kusakabe, T., Honda, D., Watanabe, Y., Takeda, K., Tanaka, O., and Imai, H
Mem. Konan Univ., Sci. & Eng. Ser 60 ( 1 ) 11 - 19 2013
Joint Work
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Implications for proteasome nuclear localization revealed by the structure of the nuclear proteasome tether protein Cut8
Takeda, K., Tonthat, N., Glover, T., Xu, W., Koonin, E., Yanagida, M., and Schumacher, M.
Proc Natl Acad Sci U S A 108 ( 41 ) 16950 - 16955 2011.10
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Mis17 is a regulatory module of the Mis6-Mal2-Sim4 centromere complex that is required for the recruitment of CenH3/CENP-A in fission yeast.
Shiroiwa Y, Hayashi T, Fujita Y, Villar-Briones A, Ikai N, Takeda K, Ebe M, Yanagida M
PloS one 6 ( 3 ) e17761 2011.3
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Mis17 is a regulatory models of the Mis6-Mal2-Sim4 centromere complex that is required for the recruitment of CenH3/CENP-Ain fission yeast Reviewed
Shiroiwa, Y., Hayashi, T., Fujita, Y., Villar-Briones, A., Ikai, N., Takeda, K., Ebe, M., and Yanagida, M.
PLoS One 6 ( 3 ) 2011
Joint Work
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In quiescence of fission yeast, autophagy and the proteasome collaborate for mitochondrial maintenance and longevity
Takeda, K., and Yanagida, M.
Autophagy 6 ( 4 ) 564 - 565 2010.5
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Synergistic roles of the proteasome and autophagy for mitochondrial maintenance and chronological lifespan in fission yeast
Takeda, K., Yoshida, T., Kikuchi, S., Nagao, K., Kokubu, A., Pluskal, T., Villar-Briones, A., Nakamura, T., and Yanagida, M.
Proc Natl Acad Sci U S A 107 ( 8 ) 3540 - 3545 2010.2
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Genetic control of cellular quiescence in S. pombe
Sajiki, K., Hatanaka, M., Nakamura, T., Takeda, K., Shimanuki, M., Yoshida, T., Hanyu, Y., Hayashi, T., Nakaseko, Y., and Yanagida, M.
J Cell Sci 122 ( Pt 9 ) 1418 - 1429 2009.5
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Characterization of Schistosoma mansoni Sds homologue, a leucine-rich repeat protein that interacts with protein phosphatase type 1 and interrupts a G2/M cell-cycle checkpoint
Daher, W., Cailliau, K., Takeda, K., Pierrot, C., Khayath, N., Dissous, C., Capron, M., Yanagida, M., Browaeys, E., and Khalife, J.
Biochem J 395 ( 2 ) 433 - 441 2006.4
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Regulation of nuclear proteasome by Rhp6/Ubc2 through ubiquitination and destruction of the sensor and anchor Cut8
Takeda, K., and Yanagida, M.
Cell 122 ( 3 ) 393 - 405 2005.8
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Fission yeast living mitosis visualized by GFP-tagged gene products Reviewed
Tatebe, H., Goshima, G., Takeda, K., Nakagawa, T., Kinoshita, K., and Yanagida, M
Micron 32 67 - 74 2000
Joint Work