名古屋市立大学大学院 理学研究科 総合生命理学部

Japanese English

名古屋市立大学大学院 理学研究科 総合生命理学部

Japanese English
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名古屋市立大学大学院 理学研究科 総合生命理学部

Japanese English

Faculty Members

Kunio NAKATSUKASA

Division
Biological Science, Associate Professor
Academic Degree
Doctor of Science
Research FieldMetabolic biochemistry
KeywordsEndoplasmic reticulum, Protein quality control, Ubiquitin, Proteasome, Organelle, Metabolic pathway, Metabolism
Current Research TopicsOur primary interest is to understand the molecular mechanisms of protein quality control in organelle homeostasis and metabolism. These studies will contribute to a number of scientific areas including the development of metabolic engineering in microorganisms, an understanding of clinical diseases of protein misfolding and the regulation of cell homeostasis during different metabolic conditions.

(1) Protein quality control. Molecular machineries of endoplasmic reticulum-associated degradation (ERAD).
(2) Roles of protein degradation and post-translational modifications in regulation of metabolic pathways.
Selected Publications

(Original papers)

Cul5-type Ubiquitin Ligase KLHDC1 Contributes to the Elimination of Truncated SELENOS Produced by Failed UGA/Sec Decoding. iScience Mar 27;23(3):100970. doi: 10.1016/j.isci.2020.100970. Epub 2020 Mar 7. (2020)

Msp1 Clears Mistargeted Proteins by Facilitating Their Transfer from Mitochondria to the ER. Mol. Cell Oct 3;76(1):191-205.e10. doi: 10.1016/j.molcel.2019.07.006. Epub 2019 Aug 21. (2019)

Harmonizing experimental data with modeling to predict membrane protein insertion in yeast. Biophys. J. Aug 20;117(4):668-678. doi: 10.1016/j.bpj.2019.07.013. Epub 2019 Jul 16. (2019)

Heterologous expression and functional analysis of the F-box protein Ucc1 from other yeast species in Saccharomyces cerevisiae. J. Biosci. Bioeng. Dec;128(6):704-709. doi: 10.1016/j.jbiosc.2019.06.003. Epub 2019 Jun 25. (2019)

Hepatic Sdf2l1 controls feeding-induced ER stress and regulates metabolism. Nat. Commun. volume 10, Article number: 947, 10.1038/s41467-019-08591-6 (2019).

The HECT-type ubiquitin ligase Tom1 contributes to the turnover of Spo12, a component of the FEAR network, in G2/M phase. FEBS Letters Apr 23. doi: 10.1002/1873-3468.13066. [Epub ahead of print] (2018).

Transmembrane helix hydrophobicity is an energetic barrier during the retrotranslocation of integral membrane ERAD substrates. Mol. Biol. Cell Jul 15;28(15):2076-2090. doi: 10.1091/mbc.E17-03-0184. Epub May 24 (2017).

ASB7 regulates spindle dynamics and genome integrity by targeting DDA3 for proteasomal degradation. J. Cell. Biol. 215, 95-106 (2016).

Subcellular Fractionation Analysis of the Extraction of Ubiquitinated Polytopic Membrane Substrate during ER-Associated Degradation. PLOS ONE 11(2):e0148327. doi: 10.1371/journal.pone.0148327 (2016).

The Ubiquitin Ligase SCFUcc1 Acts as a Metabolic Switch for the Glyoxylate Cycle. Mol. Cell 59, 22-34 (2015).

The nutrient stress-induced small GTPase Rab5 contributes to the activation of vesicle trafficking and vacuolar activity. J. Biol. Chem. 289, 20970-20978 (2014).

A stalled retrotranslocation complex reveals physical linkage between substrate recognition and proteasomal degradation during ER-associated degradation. Mol. Biol. Cell 24, 1765-1775 (2013).

Non-SCF-type F-box protein Roy1/Ymr258c interacts with a Rab5-like GTPase Ypt52 and inhibits Ypt52 function. Mol. Biol. Cell 22, 1575-1584 (2011).

Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell 132, 101-112 (2008).

(Review articles)
Proteolytic regulation of metabolic enzymes by E3 ubiquitin ligase complexes: lessons from yeast. Crit. Rev. Biochem. Mol. Biol. 50, 489-502 (2015).

Recent technical developments in the study of ER-associated degradation. Curr. Opin. Cell Biol. 29, 82-91 (2014).

The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum. Traffic 9, 861-870 (2008).