PDI Family Members as Guides for Client Folding and Assembly |
| |
| Authors: | Shingo Kanemura Motonori Matsusaki Kenji Inaba Masaki Okumura |
| |
| Affiliation: | 1.School of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda, Hyogo 669-1337, Japan;2.Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai, Miyagi 980-8577, Japan; (M.M.); (K.I.);3.Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3 Aramakiaza Aoba, Aoba-ku, Sendai, Miyagi 980-8578, Japan |
| |
| Abstract: | Complicated and sophisticated protein homeostasis (proteostasis) networks in the endoplasmic reticulum (ER), comprising disulfide catalysts, molecular chaperones, and their regulators, help to maintain cell viability. Newly synthesized proteins inserted into the ER need to fold and assemble into unique native structures to fulfill their physiological functions, and this is assisted by protein disulfide isomerase (PDI) family. Herein, we focus on recent advances in understanding the detailed mechanisms of PDI family members as guides for client folding and assembly to ensure the efficient production of secretory proteins. |
| |
| Keywords: | endoplasmic reticulum (ER) protein disulfide isomerase (PDI) family redox disulfide protein folding assembly disassembly |
|
|
