PUBLICATIONS
Eiyama A., Onishi M., Omi Y., Nagumo S., Nakatsukasa K., and Okamoto K.
ER-associated degradation by Doa10 restrains mitophagy in yeast
bioRxiv (Posted on April 09, 2024).
Ikeda T., Yamazaki K., Okumura F., Kamura T.*, and Nakatsukasa K.*
Role of the San1 ubiquitin ligase in the heat stress-induced degradation of non-native Nup1 in the nuclear pore complex
Genetics (2024) Feb 1:iyae017. doi: 10.1093/genetics/iyae017. Online ahead of print.
Hayashi M., Kawarasaki T., and Nakatsukasa K.*
Degradation of citrate synthase lacking the mitochondrial targeting sequence is inhibited in cells defective in Hsp70/Hsp40 chaperones under heat stress conditions
FEMS Yeast Research (2023) Dec 21:foad054. doi: 10.1093/femsyr/foad054. Online ahead of print.
Nishio K.† , Kawarasaki T.† , Sugiura Y.† , Matsumoto S., Konoshima A., Takano Y., Hayashi M., Okumura F., Kamura T.*, Mizushima T.*, and Nakatsukasa K.*
†: These authors equally contributed to this work.
*: Corresponding authors
Defective import of mitochondrial metabolic enzyme elicits ectopic metabolic stress
Science Advances (2023) Apr 14;9(15):eadf1956. doi: 10.1126/sciadv.adf1956. Epub 2023 Apr 14. 日本語の解説はこちら。
Takano Y. and Nakatsukasa K.*
Hydroxyurea inhibits ERAD-L independently of S-phase arrest in budding yeast
bioRxiv (Posted on January 23, 2023)
Kawarasaki T. and Nakatsukasa K.*
Metabolomics analysis of an AAA-ATPase Cdc48-deficient yeast strain
Heliyon (2023) Jan 24;9(2):e13219. doi: 10.1016/j.heliyon.2023.e13219. eCollection 2023 Feb.
Nakatsukasa K.*, Fujisawa M., Yang X., Kawarasaki T., Okumura F., and Kamura T.*
Triacylglycerol lipase Tgl4 is a stable protein and its dephosphorylation is regulated in a cell cycle-dependent manner in Saccharomyces cerevisiae
Biochemical and Biophysical Research Communications (2022) Aug 11; doi.org/10.1016/j.bbrc.2022.08.022
Obara K., Yoshikawa T., Yamaguchi R., Kuwata K., Nakatsukasa K., Nishimura K., and Kamura T.
Proteolysis of adaptor protein Mmr1 during budding is necessary for mitochondrial homeostasis in Saccharomyces cerevisiae
Nature Communications (2022) Apr 14;13(1):2005. doi: 10.1038/s41467-022-29704-8.
Kusama K., Suzuki Y., Kurita E., Kawarasaki T., Obara K., Okumura F., Kamura T.*, and Nakatsukasa K.*
Dot6/Tod6 degradation fine-tunes the repression of ribosome biogenesis under nutrient-limited conditions
iScience (2022) Feb 26; 25(3):103986. doi: 10.1016/j.isci.2022.103986. eCollection 2022 Mar 18. 日本語の解説はこちら。
Nakatsukasa K.*, Wigge S., Takano Y., Kawarasaki T., Kamura T., and Brodsky J.L.*
A positive genetic selection for transmembrane domain mutations in HRD1 underscores the importance of Hrd1 complex integrity during ERAD
Current Genetics (2022) Jan 18. doi: 10.1007/s00294-022-01227-1. Online ahead of print.
Okumura F., Oki N., Fujiki Y., Ikuta R., Osaki K., Hamada S., Nakatsukasa K., Hisamoto N., Hara T., Kamura T.
ZSWIM8 is a myogenic protein that partly prevents C2C12 differentiation
Scientific Reports (2021) Oct 22;11(1):20880. doi: 10.1038/s41598-021-00306-6.
*Nakatsukasa K.
Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast
International Journal of Molecular Sciences (2021), 22(3), 1061; https://doi.org/10.3390/ijms22031061 (registering DOI)
Okumura F., Fujiki Y., Oki N., Osaki K., Nishikimi A., Fukui Y., Nakatsukasa K., and Kamura T.
Cul5-type Ubiquitin Ligase KLHDC1 Contributes to the Elimination of Truncated SELENOS Produced by Failed UGA/Sec Decoding
iScience (2020) Mar 27;23(3):100970. doi: 10.1016/j.isci.2020.100970. Epub 2020 Mar 7.
Matsumoto S., Nakatsukasa K., Kakuta C., Tamura Y., Esaki M., and *Endo T.
Msp1 Clears Mistargeted Proteins by Facilitating Their Transfer from Mitochondria to the ER
Molecular Cell (2019) Oct 3;76(1):191-205.e10. doi: 10.1016/j.molcel.2019.07.006. Epub 2019 Aug 21. (Press release in Japanese)
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.
Harmonizing experimental data with modeling to predict membrane protein insertion in yeast
Biophysical Journal (2019) Aug 20;117(4):668-678. doi: 10.1016/j.bpj.2019.07.013. Epub 2019 Jul 16.
*Nakatsukasa K., Kawarasaki T., and Moriyama A.
Heterologous expression and functional analysis of the F-box protein Ucc1 from other yeast species in Saccharomyces cerevisiae
Journal of Bioscience and Bioengineering (2019) Dec;128(6):704-709. doi: 10.1016/j.jbiosc.2019.06.003. Epub 2019 Jun 25.
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.
Hepatic Sdf2l1 controls feeding-induced ER stress and regulates metabolism
Nature Communications (2019) volume 10, Article number: 947, 10.1038/s41467-019-08591-6
*Nakatsukasa K., Sone M., Alemayehu D.H., Okumura F., and *Kamura T.
The HECT-type ubiquitin ligase Tom1 contributes to the turnover of Spo12, a component of the FEAR network, in G2/M phase.
FEBS Letters (2018) May;592(10):1716-1724. doi: 10.1002/1873-3468.13066. Epub 2018 May 7.
*Okumura F., Joo-Okumura A., Obara K., Petersen A., Nishikimi A., Fukui Y., Nakatsukasa K., and *Kamura T.
Ubiquitin ligase SPSB4 diminishes cell repulsive responses mediated by EphB2.
Molecular Biology of the Cell (2017) Nov 15;28(24):3532-3541. doi: 10.1091/mbc.E17-07-0450. Epub 2017 Sep 20.
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.
Transmembrane helix hydrophobicity is an energetic barrier during the retrotranslocation of integral membrane ERAD substrates.
Molecular Biology of the Cell (2017) Jul 15;28(15):2076-2090. doi: 10.1091/mbc.E17-03-0184. Epub 2017 May 24.
*Okumura F., Joo-Okumura A., Nakatsukasa K., and *Kamura T.
Hypoxia-inducible factor-2α stabilizes the von Hippel-Lindau (VHL) disease suppressor, Myb-related protein 2.
PLOS ONE (2017) Apr 10;12(4): e0175593. doi: 10.1371/journal.pone.0175593. eCollection.
Uematsu K., *Okumura F., Tonogai S., Joo-Okumura A., Hailu A.D., Nishikimi A., Fukui Y., Nakatsukasa K., and *Kamura T.
ASB7 regulates spindle dynamics and genome integrity by targeting DDA3 for proteasomal degradation.
Journal of Cell Biology (2016) Oct 10;215(1):95-106.
*Okumura, F., Joo-Okumura, A., Nakatsukasa, K., and *Kamura, T.
The role of Cullin 5-containing ubiquitin ligases.
Cell division (2016) Mar 9;11:1. doi: 10.1186/s13008-016-0016-3. eCollection.
*Okumura, F., Uematsu K., Byrne S.D., Hirano M., Joo-Okumura A., Nishikimi A., Shuin T., Fukui Y., Nakatsukasa K., and *Kamura T.
Parallel regulation of VHL disease by pVHL-mediated degradation of B-Myb and HIF-α.
Molecular and Cellular Biology (2016) May 31;36(12):1803-17. doi: 10.1128/MCB.00067-16.
*Nakatsukasa, K. (Co-corresponding author), and *Kamura, T.
Subcellular Fractionation Analysis of the Extraction of Ubiquitinated Polytopic Membrane Substrate during ER-Associated Degradation.
PLOS ONE (2016) Feb 5;11(2): e0148327. doi: 10.1371/journal.pone.0148327. eCollection.
*Nakatsukasa, K. (Co-corresponding author) and *Kamura T.
ユビキチンリガーゼ複合体SCFUcc1はグリオキシル酸回路の代謝スイッチとして機能する
ライフサイエンス新着レビュー First Authors’ (2015).
*Nakatsukasa, K. (Co-corresponding author), Okumura, F., *Kamura, T.
Proteolytic regulation of metabolic enzymes by E3 ubiquitin ligase complexes: lessons from yeast.
Critical Reviews in Biochemistry and Molecular Biology (2015) Nov-Dec;50(6):489-502. doi: 10.3109/10409238.2015.1081869. Epub 2015 Sep 11. (Invited review)
*Nakatsukasa, K. (Co-corresponding author) and *Kamura T.
SCFUcc1ユビキチンリガーゼはグリオキシル酸回路の代謝スイッチとして機能する
実験医学 (2015) vol. 33, 2613-2616.
*Nakatsukasa, K., Nishimura, T., Byrne, S.D., Okamoto, M., Takahashi-Nakaguchi, A., Chibana, H., Okumura, F., and *Kamura, T.
The Ubiquitin Ligase SCFUcc1 Acts as a Metabolic Switch for the Glyoxylate Cycle.
Molecular Cell (2015) 59, 22-34.
*Nakatsukasa, K. and Kamura T.
BMB2015 (2015) ＠神戸「Fボックスタンパク質Ucc1による代謝制御機構の解析」
*Nakatsukasa, K., Kamura T., *Brodsky, J.L.
Recent technical developments in the study of ER-associated degradation.
Current Opinion in Cell Biology (2014) 29:82-91. doi: 10.1016/j.ceb.2014.04.008.
*Nakatsukasa, K., Kanada, A., Matsuzaki, M., Byrne, S.D., Okumura, F., and *Kamura, T.
The nutrient stress-induced small GTPase Rab5 contributes to the activation of vesicle trafficking and vacuolar activity.
The Journal of Biological Chemistry (2014) 289, 20970-20978.
*Nakatsukasa, K., Brodsky, J.L., and *Kamura, T.
A stalled retrotranslocation complex reveals physical linkage between substrate recognition and proteasomal degradation during ER-associated degradation.
Molecular Biology of the Cell (2013) 24, 1765-1775, S1761-1768.
*Okumura, F., Okumura, A., Nakatsukasa, K., and *Kamura, T.
Elongin BC 型E3ユビキチンリガーゼと細胞機能制御
生化学 (2013) vol. 85, 76-88.
*Nakatsukasa, K.
東北大学大学院薬学研究科セミナー（稲田利文教授招聘）「細胞小器官におけるタンパク質分解系」
*Nakatsukasa, K. and Kamura T.
第86回日本生化学会大会 ＠横浜「複合体型SCFYlr224w E3リガーゼの新奇基質p40の同定」
*Okumura, F., Matsuzaki, M., Nakatsukasa, K., and *Kamura, T.
The Role of Elongin BC-Containing Ubiquitin Ligases.
Frontiers in Oncology (2012) 2, 10.
*Nakatsukasa, K. and Kamura T.
第35回日本分子生物学会大会 ＠福岡 “The dynamic and controlled assembly of the Hrd1 ubiquitin ligase complex is essential to maintain ER homeostasis”
†Liu, Y., †Nakatsukasa, K. (equal first), Kotera, M., Kanada, A., Nishimura, T., Kishi, T., Mimura, S., and *Kamura, T.
Non-SCF-type F-box protein Roy1/Ymr258c interacts with a Rab5-like GTPase Ypt52 and inhibits Ypt52 function.
Molecular Biology of the Cell (2011) 22, 1575-1584.
*Nakatsukasa, K. and Kamura T.
Cullin型E3リガーゼの機能と制御機構
実験医学 (2011) vol. 29, 1933-1937.
*Nakatsukasa, K.
Global COE Mini-symposium: Toward Systems Glycobiology-Biosynthesis and catabolism of glycoproteins. ＠名古屋 “Molecular dissection of the ER-associated degradation” (2011).
*Nakatsukasa, K.
第11回 蛋白質科学会年会 ＠大阪「ERADにおける小胞体膜ユビキチンリガーゼ複合体の機能解析」(2011).
*Nakatsukasa, K.
京都大学再生医科学研究所 2011年度 学外非常勤講師（細川暢子准教授招聘）「ERADにおけるユビキチンリガーゼ複合体の動態解析」
Nakatsukasa, K., and *Brodsky, J.L.
In vitro reconstitution of the selection, ubiquitination, and membrane extraction of a polytopic ERAD substrate.
Methods in Molecular Biology (2010) 619, 365-376.
*Nakatsukasa, K.
小胞体関連分解(ERAD)における異常タンパク質の認識と逆行輸送
生化学 (2009) vol. 81, 700-703.
Nakatsukasa, K., Huyer, G., Michaelis, S., and *Brodsky, J.L.
Dissecting the ER-associated degradation of a misfolded polytopic membrane protein.
Cell (2008) 132, 101-112.
F1000Primeで取り上げられています
Nakatsukasa, K., and *Brodsky, J.L.
The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum.
Traffic (2008) 9, 861-870.
*Nakatsukasa, K.
BMB2008（第31回日本分子生物学会年会・第31回日本生化学会大会合同大会）「膜タンパク質の小胞体関連分解」
*Nakatsukasa, K.
熊本大学発生医学研究センター・第112回発生研セミナー（小椋光教授招聘）“Dissecting the ER-associated degradation of a misfolded membrane proteins” (2008).
*Nakatsukasa, K.
G-COE International Symposium on Frontier of Organelle Dynamics and Protein Functions, Nagoya, Japan “Dissecting the ER-Associated Degradation of a Misfolded Polytopic Membrane Protein” (2008).
Ahner, A., Nakatsukasa, K., Zhang, H., Frizzell, R.A., and *Brodsky, J.L.
Small heat-shock proteins select deltaF508-CFTR for endoplasmic reticulum-associated degradation.
Molecular Biology of the Cell (2007) 18, 806-814.
Nakatsukasa, K., and *Brodsky J.L.
The Role of BiP/Kar2p in the translocation of Proteins Across the ER membrane.
The Enzymes (2007) (Academic press, Inc.) edited by Dalbey R.E., Koehler C.M., and Tamanoi F.
*Nakatsukasa, K.
分子生物学会2006フォーラム“Reconstitution of the ubiquitination of misfolded multispanning membrane proteins” (2006).
*Nakatsukasa, K.
タンパク質のOマンノシル化と小胞体品質管理
実験医学 (2005) vol. 23, 2333-2337.
*Nishikawa, S., Brodsky, J.L., and Nakatsukasa, K.
Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD).
Journal of Biochemistry (2005) 137, 551-555.
Nakatsukasa, K., and *Brodsky, J.L.
The American Society of Cell Biology 45th Annual Meeting@San Francisco “Role of chaperones in recognizing substrate for ER-associated degradation (ERAD), determined by in vitro reconstitution of Ste6p* ubiquitination” (2005). 英語口頭発表
Nishikawa, S., Nakatsukasa, K., and *Endo, T.
小胞体品質管理におけるシャペロンと糖鎖の役割?何が異常で何を除去すべきか
蛋白質核酸酵素 (2004) vol. 49, 988-991.
Nakatsukasa, K., Okada, S., Umebayashi, K., Fukuda, R., Nishikawa, S., and *Endo, T.
Roles of O-mannosylation of aberrant proteins in reduction of the load for endoplasmic reticulum chaperones in yeast.
The Journal of Biological Chemistry (2004) 279, 49762-49772.
Nakatsukasa, K., Nishikawa, S., Hosokawa, N., Nagata, K., and *Endo, T.
Mnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins.
The Journal of Biological Chemistry (2001) 276, 8635-8638.