Yoshiaki Azuma

Associate Professor
Primary office:
(785) 864-7540
3037 Haworth Hall


The role of posttranslational modification by SUMO on cell division cycle.

Posttranslational protein modification modulates the biochemical and cell biological function of the proteins and has essential role to regulate various physiological phenomena. SUMO family of protein is small ubiquitin-related protein that modifies various cellular proteins to be conjugated to substrates in a manner similar to Ubiquitin (SUMO modification). Genetic analysis indicates that SUMO modification is essential for viability in eukaryote. Defect in SUMO modification caused aberrant mitosis in yeast and fruit fly, suggesting the SUMO modification pathway is involved in proper progression of mitosis. I have found that mitotic specific SUMO modification has crucial role in chromosome segregation by using Xenopus egg extracts in vitro cell cycle assay system. My lab will focus on understanding a role of mitotic SUMO modification in respect to chromosome segregation, especially, the function of SUMO modification on DNA topoisomerase II (TopoII), which is a major SUMO modified substrate in mitosis. During mitosis, chromosomes dramatically change their structure to organize proper structure for mitotic chromosome. This event is essential to separate sister chromosomes faithfully in anaphase of mitosis. TopoII is one of the key enzymes to organize proper chromosome structure, thus SUMO modification of TopoII suggested to have important role of regulation of chromosomal structure during mitosis. My lab will utilize Xenopus egg extracts in vitro cell cycle assay to study biochemical and cell biological function of mitotic SUMO modification.

Teaching Interests

  • Cell biology
  • Biochemistry

Research Interests

  • Cell cycle
  • SUMOylation

Selected Publications

Yoshida, M. M, & Azuma, Y. (2016). Mechanisms behind Topoisomerase II SUMOylation in chromosome segregation. Cell Cycle.

Yoshida, M. M, Ting, L., Gygi, S. P, & Azuma, Y. (2016). SUMOylation of DNA topoisomerase IIα regulates histone H3 kinase Haspin and H3 phosphorylation in mitosis. Journal of Cell Biology, 213(6), 665-78.

Sridharan, V., & Azuma, Y. (2016). SUMO-interacting motifs (SIMs) in Polo-like kinase 1-interacting checkpoint helicase (PICH) ensure proper chromosome segregation during mitosis. Cell Cycle.

Ryu, H., Yoshida, M. M, Sridharan, V., Kumagai, A., Dunphy, W. G, Dasso, M., & Azuma, Y. (2015). SUMOylation of the C-terminal domain of DNA topoisomerase IIα regulates the centromeric localization of Claspin. Cell Cycle.

Sridharan, V., Park, H., Ryu, H., & Azuma, Y. (2015). SUMOylation regulates Polo-like kinase 1-interacting checkpoint helicase (PICH) during mitosis. the Journal of Biological Chemistry.

Sudharsan, R., & Azuma, Y. (2012). The SUMO ligase PIAS1 regulates UV-induced apoptosis by recruiting Daxx to SUMOylated foci. J Cell Sci, 125, 5819-5829.

Ryu, H., Al-Ani, G., Deckert, K., Kirkpatrick, D., Gygi, S. P., Dasso, M., & Azuma, Y. (2010). PIASy mediates SUMO-2/3 conjugation of poly (ADP-ribose) polymerase1 (PARP1) on mitotic chromosomes. J Biol Chem, 285, 14415-14423.

Ryu, H., Furuta, M., Kirkpatrick, D., Gygi, S. P., & Azuma, Y. (2010). PIASy-dependent SUMOylation regulates DNA topoisomerase IIα activity. J Cell Biol, 191, 783-794. DOI:10.1083/jcb.201004033 http://hdl.handle.net/1808/13490

» Show All Publications

Representative Publications

Yoshida, M.M., Ting, L., Gygi, S.P., and Azuma, Y. (2016). SUMOylation of DNA topoisomerase IIalpha regulates histone H3 kinase Haspin and H3 phosphorylation in mitosis. J Cell Biol 213, 665-678.

Ryu, H., Yoshida, M.M., Sridharan, V., Kumagai, A., Dunphy, W.G., Dasso, M., and Azuma, Y. (2015). SUMOylation of the C-terminal domain of DNA topoisomerase IIalpha regulates the centromeric localization of Claspin. Cell Cycle 14, 2777-2784.

Sridharan, V., Park, H., Ryu, H., and Azuma, Y. (2015). SUMOylation Regulates Polo-like Kinase 1-interacting Checkpoint Helicase (PICH) during Mitosis. J Biol Chem 290, 3269-3276.

Ryu, H., Gygi, S.P., Azuma, Y., Arnaoutov, A., and Dasso, M. (2014). SUMOylation of Psmd1 Controls Adrm1 Interaction with the Proteasome. Cell Rep 7, 1842-1848.

Al-Ani, G., Briggs, K., Malik, S.S., Conner, M., Azuma, Y., and Fischer, C.J. (2014). Quantitative Determination of Binding of ISWI to Nucleosomes and DNA Shows Allosteric Regulation of DNA Binding by Nucleotides. Biochemistry 53, 4334-4345.

Sudharsan, R. and Azuma, Y. (2012) The SUMO ligase PIAS1 regulates UV-induced apoptosis by recruiting Daxx to SUMOylated foci. J Cell Sci 125, 5819-5829

Ryu, H., Furuta, M., Kirkpatrick, D., Gygi, S. P., and Azuma, Y. (2010) PIASy-dependent SUMOylation regulates DNA topoisomerase II{alpha} activity, J Cell Biol 191, 783-794.

Ryu, H., and Azuma, Y. (2010) Rod/Zw10 complex is required for PIASy-dependent centromeric SUMOylation, J Biol Chem 285, 32576-32585.

Ryu, H., Al-Ani, G., Deckert, K., Kirkpatrick, D., Gygi, S. P., Dasso, M., and Azuma, Y. (2010) PIASy mediates SUMO-2/3 conjugation of poly(ADP-ribose) polymerase 1 (PARP1) on mitotic chromosomes, J Biol Chem 285, 14415-14423.

 Azuma, Y. (2009) Analysis of SUMOylation of topoisomerase IIalpha with Xenopus egg extracts, Methods Mol Biol 582, 221-231.

 Wang, Y., Azuma, Y., Moore, D., Osheroff, N., and Neufeld, K. L. (2008) Interaction between tumor suppressor adenomatous polyposis coli and topoisomerase IIalpha: implication for the G2/M transition, Mol Biol Cell 19, 4076-4085.

 Diaz-Martinez, L. A., Gimenez-Abian, J. F., Azuma, Y., Guacci, V., Gimenez-Martin, G., Lanier, L. M., and Clarke, D. J. (2006) PIASgamma is required for faithful chromosome segregation in human cells, PLoS ONE 1, e53.

 Azuma, Y., Arnaoutov, A., Anan, T., and Dasso, M. (2005) PIASy mediates SUMO-2 conjugation of Topoisomerase-II on mitotic chromosomes, Embo J 24, 2172-2182.

 Azuma, Y., Arnaoutov, A., and Dasso, M. (2003) SUMO-2/3 regulates topoisomerase II in mitosis, J Cell Biol 163, 477-487.

 Azuma, Y., Tan, S. H., Cavenagh, M. M., Ainsztein, A. M., Saitoh, H., and Dasso, M. (2001) Expression and regulation of the mammalian SUMO-1 E1 enzyme, Faseb J 15, 1825-1827.

 Azuma, Y., Renault, L., Garcia-Ranea, J. A., Valencia, A., Nishimoto, T., and Wittinghofer, A. (1999) Model of the ran-RCC1 interaction using biochemical and docking experiments, J Mol Biol 289, 1119-1130.

 Azuma, Y., Hachiya, T., and Nishimoto, T. (1997) Inhibition by anti-RCC1 monoclonal antibodies of RCC1-stimulated guanine nucleotide exchange on Ran GTPase, J Biochem (Tokyo) 122, 1133-1138.

 Azuma, Y., Seino, H., Seki, T., Uzawa, S., Klebe, C., Ohba, T., Wittinghofer, A., Hayashi, N., and Nishimoto, T. (1996) Conserved histidine residues of RCC1 are essential for nucleotide exchange on Ran, J Biochem (Tokyo) 120, 82-91.


Home to 50+ departments, centers, and programs, the School of the Arts, and the School of Public Affairs and Administration
KU offers courses in 40 languages
No. 1 ranking in city management and urban policy —U.S. News and World Report
One of 34 U.S. public institutions in the prestigious Association of American Universities
Nearly $290 million in financial aid annually
44 nationally ranked graduate programs.
—U.S. News & World Report
Top 50 nationwide for size of library collection.
—ALA
23rd nationwide for service to veterans —"Best for Vets," Military Times
KU Today