Kayoko Tanaka

Direct contact details

Tel: +44 (0)116 229 7126

Personal details

  • Ph.D: University of Tokyo 1995.
  • 1995-1998: Post-doctoral Fellow, University of Geneva.
  • 1998-2002: Post-doctoral Fellow, University of Manchester/Paterson Institute for Cancer Research.
  • 2002-2005: Senior Research Associate, University of Tokyo.
  • 2005-2006: Lecturer, University of Tokyo.
  • Nov 2006 -: Lecturer, Department of Biochemistry, University of Leicester.


  • Tanaka K. 2014. Centrosome duplication: suspending a license by phosphorylating a template. Curr Biol., 24 R651-653.
  • Dhani DK, Goult BT, George GM, Rogerson DT, Bitton DA, Miller CJ, Schwabe JW, Tanaka K. 2013. Mzt1/Tam4, a fission yeast MOZART1 homologue, is an essential component of the γ-tubulin complex and directly interacts with GCP3Alp6Mol Biol Cell, 24, 3337-3349.
  • Varadarajan S, Tanaka K, Smalley JL, Bampton ETW, Pellecchia M, Dinsdale D, Willars GB, Cohen GM. 2013. Endoplasmic Reticulum Membrane Reorganization Is Regulated by Ionic Homeostasis. PLoS ONE, 8, e56603
  • Grallert A, Chan KY, Alonso-Nunez ML, Madrid M, Biswas A, Alvares-Tabares I, Connolly Y, Tanaka K, Robertson A, Ortiz JM, Smith DL, Hagan IM. 2013. Removal of Centrosomal PP1 by NIMA Kinase Unlocks the MPF Feedback Loop to Promote Mitotic Commitment in S.pombe. Curr. Biol., 23, 213-222.
  • Varadarajan S, Bampton ET, Smalley JL, Tanaka K, Caves RE, Butterworth M, Wei J, Pellecchia M, Mitcheson J, Gant TW, Dinsdale D, Cohen GM. 2012. A novel cellular stress response characterised by a rapid reorganisation of membranes of the endoplasmic reticulum. Cell Death Differ., 19, 1896-1907.
  • Funaya C, Samarasinghe S, Pruggnaller S, Ohta M, Connolly Y, Müller J, Murakami H, Grallert A, Yamamoto M, Smith D, Antony C, Tanaka K. 2012. Transient structure associated with the spindle pole body directs meiotic microtubule reorganization in S.pombe. Curr. Biol., 22, 562-574.
  • Kakui Y, Sato M, Tanaka K, Yamamoto M. 2011. A novel fission yeast mei4 mutant that allows efficient synchronization of telomere dispersal and the first meiotic division. Yeast28, 467-479.
  • Arai K, Sato M, Tanaka K, Yamamoto M. 2010. Nuclear compartmentalization is abolished during fission yeast meiosis. Curr Biol., 20, 1913-1918.
  • Kohda TA, Tanaka K, Konomi M, Sato M, Osumi M, Yamamoto M. 2007. Fission yeast autophagy induced by nitrogen starvation generates a nitrogen source to drive the adaptation processes. Genes to cells, 12, 155-170.
  • Harigaya Y, Tanaka H, Yamanaka S, Tanaka K, Watanabe Y, Tsutsumi C, Chikashige Y, Hiraoka Y, Yamashita A, Yamamoto M. 2006. Selective elimination of messenger RNA prevents an incidence of untimely meiosis. Nature442, 45-50.
  • Tanaka K, Kohda T, Yamashita A, Nonaka N, Yamamoto M. 2005. Hrs1p/Mcp6p on the meiotic SPB organizes astral microtubule arrays for oscillatory nuclear movement. Curr. Biol., 15, 1479-1486.
  • Hirota K, Tanaka K, Ohta K, Yamamoto M. 2003. Gef1p and Scd1p, the Two GDP-GTP exhange factors for Cdc42p, form a ring structure that shrinks during cytokinesis in Schizosaccharomyces pombe. Mol. Biol. Cell14, 3617-3627.
  • MacIver FH*, Tanaka K*, Robertson AM, Hagan IM. 2003. Physical and functional interactions between polo kinase and the spindle pole component Cut12 regulate mitotic commitment in S.pombe. Genes Dev., 17, 1507-1523. (* These authors made equal contributions)
  • Tanaka K, Petersen J, MacIver F, Mulvihill DP, Glover DM, Hagan IM. 2001. The role of Plo1 kinase in mitotic commitment and septation in Schizosaccharomyces pombe. EMBO J. 20, 1259-1270.
  • Hirota K, Tanaka K, Watanabe Y, Yamamoto M. 2001. Functional analysis of the C-terminal cytoplasmic region of the M-factor receptor in fission yeast. Genes Cells 6, 201-214.
  • Mayor T, Stierhof Y-D, Tanaka K, Fry AM, Nigg EA. 2000. The centrosomal protein C-Nap1 is required for cell cycle-regulated centrosome cohesion. J. Cell Biol. 151, 837-846.
  • Sillije HH, Takahashi K, Tanaka K, Van Houwe G, Nigg EA. 1999. Mammalian homologues of the plant Tousled gene code for cell-cycle-regulated kinases with maximal activities linked to ongoing DNA replication. EMBO J. 18. 5691-5702.
  • Tanaka K, Nigg EA. 1999. Cloning and Characterization of the Murine Nek3 Protein Kinase, a Novel Member of the NIMA Family of Putative Cell Cycle Regulators. J. Biol. Chem. 274. 13491-13497.
  • Fry AM, Mayor T, Meraldi P, Stierhof Y-D, Tanaka K, Nigg EA. 1998. C-Nap1, a novel centrosomal coiled-coil protein and candidate substrate of the cell cycle-regulated protein kinase Nek2. J. Cell Biol. 141, 1563-1574.
  • Tanaka K, Parvinen M, Nigg EA. 1997. The in vivo expression pattern of mouse Nek2, a NIMA-related kinase, indicates a role in both mitosis and meiosis. Exp. Cell Res. 237, 264-274.
  • Tanaka K, Davey J, Imai Y, Yamamoto M. 1993. Schizosaccharomyces pombe map3+ Encodes the Putative M-Factor Receptor. Mol. Cell. Biol. 13, 80-88.


Microtubule re-organisation and cell signalling associated with meiotic differentiation

Sexual differentiation involving mating and meiosis is fundamental to living organisms to achieve effective evolution. Gametes generated through meiosis contain a set of genetic materials, which are different from their parents, through extensive chromosome pairing and recombination, followed by two successive rounds of chromosome segregation without intervening DNA synthesis.

Our research aims to understand the highly coordinated sexual differentiation process. We focus on two subjects; (1) function and regulation of microtubules during meiotic prophase I and (2) the mechanism of cell signaling that triggers meiotic differentiation. We exploit genetically tractable fission yeast as a powerful model system to address these questions.

(1) Molecular mechanism of microtubule reorganization during sexual differentiation.

Nuclear movement that involves nuclear rotation and chromosome movement during meiotic prophase I is highly conserved from yeast to mammals. It facilitates pairing of homologous chromosomes, leading to efficient meiotic recombination. In many eukaryotes including fission yeast and mice, the movement is primarily driven by microtubule and associated motor proteins.

We showed that, during fission yeast meiotic prophase I, microtubules emanate from the area just above the yeast centrosome to form radial microtubule (rMT) structure (Fig. 1, Funaya et al., Curr. Biol., 22, 562-574 (2012)). We termed the area the radial microtubule organizing centre (rMTOC).


The rMTOC resembles the pericentriolar material (PCM) in higher eukaryotes in many ways: appearing as electron-dense structure by EM observation, being enriched in γ-tubulin within the structure, and harboring high MTOC activity (Fig2, Funaya et al., Curr. Biol., 22, 562-574 (2012)). We believe that rMTOC serves as a unique tractable model to study PCM biology.

Our projects involve identification of rMTOC components and exploration of mechanistic insights as to how rMTOC holds microtubule minus ends and how rMTOC is associated with the centrosome.

(2) Integrated understanding of RAS-mediated signaling pathways.

Fission yeast mating pheromone triggers the RAS signaling pathway essential for meiotic differentiation including mating and sporulation.

A model has been proposed that Ras1, the unique fission yeast RAS homologue, activates two downstream targets, the pheromone MAPK cascade and the Cdc42 morphological pathway, based on the result of yeast two hybrid analysis that Ras1 interacts with both MAPKKKByr2 and Scd1, a GDP-GTP exchange factor for Cdc42 (Chang et al., Cell, 79, 131-141, (1994)). However, direct in vivo biochemical evidence has been missing.

We established a condition to induce highly synchronous mating of haploid fission yeast cells and an assay system to directly measure the MAPKSpk1 activation status with an anti-phospho ERK monoclonal antibody. These tools allow us to precisely monitor the MAPKSpk1 activation status during the mating process in various mutant cells and to build up a model of Ras signaling. Our results support the original hypothesis that Ras1 activates two downstream pathways, the pheromone MAPK cascade and the Cdc42 morphological pathway (Fig. 3, manuscript in preparation). Furthermore, activation of these two pathways is not only necessary but also sufficient for successful pheromone response.

Fig. 3.  RAS signaling plays a key role in fission yeast sexual differentiation

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