Kayoko Tanaka

Personal Details

Kayoko TanakaLecturer
Kayoko Tanaka 2017pic Department: Molecular and Cell Biology
Telephone: +44 (0)116 229 7126
Email: kt96@le.ac.uk


  • 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.


  • Cell biology
  • Application of molecular genetics to study protein complexes


  1. Tanaka K. 2014. Centrosome duplication: suspending a license by phosphorylating a template. Curr Biol., 24 R651-653.
  2. 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.
  3. 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
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  8. Arai K, Sato M, Tanaka K, Yamamoto M. 2010. Nuclear compartmentalization is abolished during fission yeast meiosis. Curr Biol., 20, 1913-1918.
  9. 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.
  10. 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.
  11. 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.
  12. 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.
  13. 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)
  14. 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.
  15. 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.
  16. 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.
  17. 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.
  18. 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.
  19. 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.
  20. 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.
  21. Tanaka K, Davey J, Imai Y, Yamamoto M. 1993. Schizosaccharomyces pombe map3+ Encodes the Putative M-Factor Receptor. Mol. Cell. Biol. 13, 80-88.


Our lab has two major research interests as below.

(1) Unravelling microtubule anchoring mechanism

Microtubules (MTs), one of the major cytoskeletons, are hollow tubular structures, generated by polymerisation of a- and b- tubulin hetero-dimers. Secure attachment of MTs to their anchoring sites is essential for a range of fundamental cellular activities. A prototype MT anchoring matrix is pericentriolar material (PCM) of the centrosome (Fig.1). Its physiological significance is highlighted in nuclear migration during neural cell development, where an impaired PCM component can lead to a compromised nuclear migration and brain developmental disorders such as microcephaly.

 Centrosome picMammalian pic



Nuclear migration led by anchored MT is seen in a wide range of occasions across various organisms (Fig. 2). However, precise molecular entities of the MT anchoring matrices, structural arrangement of their components and the way a matrix securely holds the MT ends are largely unknown. We aim to address these questions by exploiting a highly tractable model organism, fission yeast.

We showed that, during fission yeast meiosis, cells develop a meiosis-specific microtubule organizing centre (MTOC) that organises radial MT (rMT) structure (Fig. 3, Funaya et al., Curr. Biol., 22, 562-574 (2012)). We termed it the rMT organizing centre (rMTOC).








The rMTOC resembles the PCM of higher eukaryotes in many ways: appearing as electron-dense structure by EM observation, being enriched in g-tubulin within the structure, and harboring high MTOC activity (Fig4, Funaya et al., Curr. Biol., 22, 562-574 (2012)). We believe that rMTOC serves as a unique tractable model to study PCM biology.

rMTOC pic2




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

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

Ras belongs to a conserved group of small GTPases, a molecular switch that is involved in cell proliferation, differentiation and survival. It acts as a signalling hub that regulates a number of downstream pathways.

Since their discovery in 1982, human RAS genes have been well established to carry oncogenic mutations in about 30% of cancers. However, the precise molecular mechanism which primes oncogenic-RAS driven tumorigenesis is not fully understood, especially because of the complexity of the RAS signaling that activates a wide range of effector pathways.

Our research goal is to reveal the mechanism of oncogenic-RAS-driven tumorigenesis at a molecular level. As a first step, we use a highly tractable model system, fission yeast, where the unique RAS homologue Ras1 was indicated to regulate two effector pathways, MAPK and Cdc42, during sexual differentiation (Chang et al., (1994)). By directly monitoring MAPK and Cdc42 activation status, we have confirmed that Ras1 does regulate these two pathways. Furthermore, we showed that these are the sole Ras1 effector pathways during sexual differentiation (Kelsall et al., manuscript in preparation, Fig. 5).

Fission yeast RAS pic

Fig. 5
. Fission yeast RAS signaling during sexual differentiation.

By exploiting this simple setting as a powerful model, we can precisely monitor the activation status of both MAPK and Cdc42 in the presence of Ras1 mutants carrying mutations equivalent of human oncogenic mutations. This approach will reveal how an “oncogenic” Ras1 interacts with the effector pathway components to trigger cellular anomalies. The information obtained through our study will shed a light on the comparable situation in human case, considering a high homology (83%) of the primary sequences between the fission yeast Ras1 and human H- and K-RAS molecules.


PhD projects are available in our lab

  • Molecular understanding of microtubule anchoring matrix
  • Molecular mechanism of oncogenic-RAS-driven Cdc42/Rac activation

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Department of Molecular and Cell Biology

T: +44(0)116 229 7038
E: MolCellBiol@le.ac.uk

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