Frontier Research Institute for Interdisciplinary Sciences
Tohoku University


Masaki Okumura

Associate professorAdvanced Basic Science

Mentor Information
Satoshi Takahashi (Institute of Multidisciplinary Research for Advanced Materials)
Research Fields Structural biology, Protein Science, Biochemistry
Research Subjects
  • Elucidation of protein quality control mechanism in the endoplasmic reticulum
Academic Society Membership Protein Science Society of Japan, The Molecular Biology Society of Japan
Research Outline  

Protein folding coupled with disulfide bond formation, that is oxidative protein folding, proceeds mainly in the endoplasmic reticulum (ER). Greater than 20 Protein Disulfide Isomerase family members (PDIs) are conserved in the mammalian ER to catalyze this reaction. However, it remains an important open question how PDIs recognize various substrates and guide their proper folding through disulfide bond formation and isomerization. The goal of this study is to understand how protein homeostasis is maintained in the mammalian ER. To this end, I employ multiple approaches including single-molecule observation by high-speed AFM, NMR/SAXS analyses in solution, X-ray crystal structure analysis, and several biochemical assays. Diabetes and neurodegenerative diseases are caused by impairment of the protein quality control systems in cells, and hence this study will provide molecular insights into the mechanism underlying these diseases.

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