Researcher Database



FacultyGraduate School of Natural Sciences Division of Biological Science
PositionAssociate Professor
Last Updated :2020/01/09

Researcher Profile and Settings


  • Doctor of Science, Nagoya University

Association Memberships


Academic & Professional Experience

  •   2015 10  - 2017 03 , Nagoya University Graduate School of Science Division of Biological Science Genetic Mechanism, Lecturer
  •   2009 04 01  - 2015 09 30 , Nagoya University, Graduate School of Science Division of Biological Science, Assistant Professor
  •   2004 04  - 2009 03 , University of Pittsburgh, Department of Biological Sciences, Post-doc

Research Activities

Research Areas

  • Agricultural chemistry, Applied biochemistry
  • Biological Science, Cell biology
  • Biological Science, Functional biochemistry


  • Msp1 Clears Mistargeted Proteins by Facilitating Their Transfer from Mitochondria to the ER, Matsumoto S., Nakatsukasa K., Kakuta C., Tamura Y., Esaki M., and *Endo T., Molecular Cell , 76, (1) 191 - 205,   2019 10 , Refereed
  • Harmonizing experimental data with modeling to predict membrane protein insertion in yeast, Guerriero C.J., Gomez Y.K., Daskivich G.J., Reutter K.R., Augustine A.A., Weiberth K.F., Nakatsukasa K., Grabe M., and *Brodsky J.L., Biophysical Journal, 117, (4) 668 - 678,   2019 08 , Refereed
  • Heterologous expression and functional analysis of the F-box protein Ucc1 from other yeast species in Saccharomyces cerevisiae , *Nakatsukasa K., Kawarasaki T., and Moriyama A., Journal of Bioscience and Bioengineering,   2019 06 , Refereed
  • Hepatic Sdf2l1 controls feeding-induced ER stress and regulates metabolism, Sasako T., Ohsugi M., Kubota N., Itoh S., Okazaki Y, Terai A., Kubota T., Yamashita S., Nakatsukasa K., Kamura T., Iwayama K., Tokuyama K., Kiyonari H., Furuta Y., Shibahara J., Fukayama M., Enooku K., Okushin K., Tsutsumi T., Tateishi R., Tobe K., Asahara H., Koike K., *Kadowaki T. & *Ueki K., Nature Communications, 10,   2019 02 , Refereed
  • The HECT-type ubiquitin ligase Tom1 contributes to the turnover of Spo12, a component of the FEAR network, in G2/M phase., *Nakatsukasa K., Sone M., Alemayehu D.H., Okumura F., and *Kamura T., 529, (10) 1716 - 1724,   2018 05 , Refereed
  • Transmembrane helix hydrophobicity is an energetic barrier during the retrotranslocation of integral membrane ERAD substrates., Guerriero C.J., Reutter K., Augustine A.A., Preston G.M., Weiberth K.F., Mackie T.D., Cleveland-Rubeor H.C., Bethel N.P., Callenberg K.M., Nakatsukasa K., Grabe M, and Brodsky J.L., Molecular Biology of the Cell , 28, (15) 2076 - 2090,   2017 07 , Refereed
  • Hypoxia-inducible factor-2α stabilizes the von Hippel-Lindau (VHL) disease suppressor, Myb-related protein 2., Okumura F., Joo-Okumura A., Nakatsukasa K., and Kamura T., PLOS ONE, 12, (4) 1 - 13,   2017 04 , Refereed
  • Ubiquitin ligase SPSB4 diminishes cell repulsive responses mediated by EphB2., Okumura F., Joo-Okumura A., Obara K., Petersen A., Nishikimi A., Fukui Y., Nakatsukasa K., and Kamura T., Molecular Biology of the Cell , 28, (24) 3532 - 3541,   2017 09 , Refereed
  • ASB7 regulates spindle dynamics and genome integrity by targeting DDA3 for proteasomal degradation., Uematsu K., Okumura F., Tonogai S., Joo-Okumura A., Hailu A.D., Nishikimi A., Fukui Y., Nakatsukasa K., and Kamura T., Journal of Cell Biology, 215, (1) 95 - 106,   2016 10 , Refereed
  • The role of Cullin 5-containing ubiquitin ligases, Okumura, F., Joo-Okumura, A., Nakatsukasa, K., and Kamura, T., Cell division, 11, (1) 1 - 16,   2016 05 , Refereed
  • Parallel regulation of VHL disease by pVHL-mediated degradation of B-Myb and HIF-α., Okumura, F., Uematsu K., Byrne S.D., Hirano M., Joo-Okumura A., Nishikimi A., Shuin T., Fukui Y., Nakatsukasa K., and Kamura T., Molecular and Cellular Biology, 36, (12) 1803 - 1817,   2016 05 , Refereed
  • Subcellular Fractionation Analysis of the Extraction of Ubiquitinated Polytopic Membrane Substrate during ER-Associated Degradation, Kunio Nakatsukasa* and Takumi Kamura, PLoS One,   2016 02 05 , Refereed
  • Proteolytic regulation of metabolic enzymes by E3 ubiquitin ligase complexes: lessons from yeast, Kunio Nakatsukasa*, Fumihiko Okumura and Takumi Kamura, Critical Reviews in Biochemistry and Molecular Biology, 50,   2015 12 , Refereed, Invited, Eukaryotic organisms use diverse mechanisms to control metabolic rates in response to changes in the internal and/or external environment. Fine metabolic control is a highly responsive, energy-saving process that is mediated by allosteric inhibition/activation and/or reversible modification of preexisting metabolic enzymes. In contrast, coarse metabolic control is a relatively long-term and expensive process that involves modulating the level of metabolic enzymes. Coarse metabolic control can be achieved through the degradation of metabolic enzymes by the ubiquitin-proteasome system (UPS), in which substrates are specifically ubiquitinated by an E3 ubiquitin ligase and targeted for proteasomal degradation. Here, we review select multi-protein E3 ligase complexes that directly regulate metabolic enzymes in Saccharomyces cerevisiae. The first part of the review focuses on the endoplasmic reticulum (ER) membrane-associated Hrd1 and Doa10 E3 ligase complexes. In addition to their primary roles in the ER-associated degradation pathway that eliminates misfolded proteins, recent quantitative proteomic analyses identified native substrates of Hrd1 and Doa10 in the sterol synthesis pathway.
  • The Ubiquitin Ligase SCFUcc1 Acts as a Metabolic Switch for the Glyoxylate Cycle, Nakatsukasa K*, Nishimura T, Byrne SD, Okamoto M, Takahashi-Nakaguchi A, Chibana H, Okumura F, Kamura T, Molecular Cell,   2015 05 13 , Refereed
  • The Nutrient Stress-Induced small GTPase Rab5 Contributes to the Activation of Vesicle Trafficking and Vacuolar Activity., *Nakatsukasa K., Kanada A., Matsuzaki M., Byrne S.D., Okumura F., and *Kamura T., The Journal of Biological Chemistry, 289,   2014 07 , Refereed
  • Recent technical development in the study of ER-associated degradation, *Nakatsukasa K., Kamura T., and *Brodsky J.L., Current Opinion in Cell Biology, 29,   2014 05 , Refereed, Invited
  • A stalled retrotranslocation complex reveals a physical linkage between substrate recognition and proteasomal degradation during ER-associated degradation., *Nakatsukasa K., Brodsky J.L., and *Kamura T., Molecular Biology of the Cell, 24,   2013 06 , Refereed
  • Regulation of cellular functions by Elongin BC based E3 ubiquitin ligase, Okumura F., Okumura A., Nakatsukasa K., and Kamura T., 85,   2013 02 , Refereed, Invited
  • The Role of Elongin BC-Containing Ubiquitin Ligases., Okumura F, Matsuzaki M, Nakatsukasa K, Kamura T., Frontiers in Molecular and Cellular Oncology,   2012 02 03
  • Non-SCF-type F-box protein Roy1/Ymr258c interacts with a Rab5-like GTPase Ypt52 and inhibits Ypt52 function, Liu Y*, Nakatsukasa K*, Kotera M, Kanada A, Nishimura T, Kishi T, Mimura S, Kamura T, Mol. Biol. Cell, 22,   2011 05 , Refereed
  • *The Recognition and Retrotranslocation of Misfolded proteins from the Endoplasmic Reticulum, Kunio Nakatsukasa, Jeffrey L. Brodsky, Traffic, 9,   2008 02 , Refereed, Invited
  • *Dissecting the ER-Associated Degradation of a Misfolded Polytopic Membrane Protein, Kunio Nakatsukasa, Jeffrey L. Brodsky, Cell, 132,   2008 01 , Refereed
  • *Small heat-shock proteins select deltaF508-CFTR for endoplasmic reticulum-associated degradation, Ahner A., Nakatsukasa K., Zhang H., Frizzell R.A., and Brodsky J.L., Mol. Biol. Cell, 18,   2007 03 , Refereed
  • Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD), Nishikawa S., Brodsky J.L., and Nakatsukasa K., J. Biochem. (Tokyo), 137,   2005 05 , Refereed, Invited
  • *Roles of O-mannosylation of aberrant proteins in reduction of the load for endoplasmic reticulum chaperones in yeast, Nakatsukasa K., Okada S., Umebayashi K., Nishikawa S., and Endo T., J. Biol. Chem., 279,   2004 11 , Refereed
  • *Mnl1p, an alpha-mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins, Nakatsukasa K., Nishikawa S., Hosokawa N., Nagata K., and Endo T., J. Biol. Chem., 276,   2001 03 , Refereed

Books etc

  • In vitro reconstitution of the Selection, Ubiquitination, and Membrane Extraction of a Polytopic ERAD Substrate, Nakatsukasa K., and Brodsky J.L., Joint Work, Springer, Methods in Molecular Biology,   2010
  • The Enzymes "The Role of BiP/Kar2p in the translocation of Proteins Across the ER membrane", Kunio Nakatsukasa, Jeffrey L. Brodsky, Joint Work, ACADEMIC PRESS,   2007

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