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JST Press Release

May 5, 2017
Japan Science and Technology Agency (JST)
5-3, Yonbancho, Chiyoda-ku, Tokyo 102-8666

Elucidation of molecular mechanisms underlying the elimination of aberrant proteins in cells

Toward overcoming neurodegenerative diseases and diabetes

ERdj5, a member of the protein disulfide isomerase (PDI) family, serves to eliminate misfolded proteins by reducing aberrantly formed disulfide bonds. This work revealed a new crystal structure and conformational dynamics of ERdj5, elucidating molecular mechanisms of protein quality control in the endoplasmic reticulum. The present findings provide molecular insights into neurodegenerative diseases and diabetes caused by accumulation of misfolded proteins.

Program Information

Research Area “Structural Life Science and Advanced Core Technologies for Innovative Life Science Research”
Research Theme “Maintenance of ER homeostasis: Crosstalks of redox regulation with calcium regulation and protein quality control in the ER”

Journal Information

Maegawa, K., Watanabe, S., Noi, K., Okumura, M., Amagai, Y., Inoue, M., Ushioda, R., Nagata, K., Ogura, T. and Inaba, K., “The highly dynamic nature of ERdj5 is key to efficient elimination of aberrant protein oligomers through ER-associated degradation”. Structure, Published online May 4, 2017, doi: 10.1016/j.str.2017.04.001.


[About Research]
Kenji Inaba, Ph.D.
Professor, Institute of Multidisciplinary Research for Advanced Materials, Tohoku University

[About Program]
Tetsu Kawaguchi
Life Innovation Group, Department of Innovation Research, JST


JST, an integrated organization of science and technology in Japan, establishes an infrastructure for the entire process from the creation of knowledge to the return to the society. For more information, visit http://www.jst.go.jp/EN/