Kunio NAKATSUKASA

	Kunio NAKATSUKASA Associate Professor, Doctor of Science
	E-mail: nakatsukasa TEL: +81-52-872-5856 FAX: +81-52-872-5856 Research Course: Biological Science
	URL http://www.nsc.nagoya-cu.ac.jp/~nakatsukasa/lab-e.html
Specialties	Metabolic biochemistry
Keywords	Endoplasmic reticulum, Protein quality control, Ubiquitin, Proteasome, Organelle, Metabolic pathway, Metabolism
Current Research	Our 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 Papers	(Original papers) 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).