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
JST CREST
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.
Contact
[About Research]
Kenji Inaba, Ph.D.
Professor, Institute of Multidisciplinary Research for Advanced Materials, Tohoku University
E-mail: 
[About Program]
Tetsu Kawaguchi
Life Innovation Group, Department of Innovation Research, JST
E-mail: 