Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding
-
- Motonori Matsusaki
- Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3, Aramakiaza Aoba, Aoba-ku, Sendai 980-8578, Japan
-
- Rina Okada
- School of Science and Technology, Kwansei Gakuin University, 2-1, Gakuen, Sanda 669-1337, Japan
-
- Yuya Tanikawa
- School of Science and Technology, Kwansei Gakuin University, 2-1, Gakuen, Sanda 669-1337, Japan
-
- Shingo Kanemura
- Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3, Aramakiaza Aoba, Aoba-ku, Sendai 980-8578, Japan
-
- Dai Ito
- Department of Brain and Cognitive Science, Daegu Gyeongbuk Institute of Science and Technology, 333, Techno Jungang Daero, Daegu 42988, Korea
-
- Yuxi Lin
- Research Center for Bioconvergence Analysis, Korea Basic Science Institute, 162, Yeongudanji-ro, Ochang-eup, Cheongwon-gu, Cheongju-si 28119, Korea
-
- Mai Watabe
- Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3, Aramakiaza Aoba, Aoba-ku, Sendai 980-8578, Japan
-
- Hiroshi Yamaguchi
- School of Science and Technology, Kwansei Gakuin University, 2-1, Gakuen, Sanda 669-1337, Japan
-
- Tomohide Saio
- Institute of Advanced Medical Sciences, Tokushima University, 3-18-15, Kuramoto-cho, Tokushima 770-8503, Japan
-
- Young-Ho Lee
- Research Center for Bioconvergence Analysis, Korea Basic Science Institute, 162, Yeongudanji-ro, Ochang-eup, Cheongwon-gu, Cheongju-si 28119, Korea
-
- Kenji Inaba
- Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai 980-8577, Japan
-
- Masaki Okumura
- Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3, Aramakiaza Aoba, Aoba-ku, Sendai 980-8578, Japan
Description
<jats:p>P5 is one of protein disulfide isomerase family proteins (PDIs) involved in endoplasmic reticulum (ER) protein quality control that assists oxidative folding, inhibits protein aggregation, and regulates the unfolded protein response. P5 reportedly interacts with other PDIs via intermolecular disulfide bonds in cultured cells, but it remains unclear whether complex formation between P5 and other PDIs is involved in regulating enzymatic and chaperone functions. Herein, we established the far-western blot method to detect non-covalent interactions between P5 and other PDIs and found that PDI and ERp72 are partner proteins of P5. The enzymatic activity of P5-mediated oxidative folding is up-regulated by PDI, while the chaperone activity of P5 is stimulated by ERp72. These findings shed light on the mechanism by which the complex formations among PDIs drive to synergistically accelerate protein folding and prevents aggregation. This knowledge has implications for understanding misfolding-related pathology.</jats:p>
Journal
-
- Biology
-
Biology 10 (11), 1112-, 2021-10-28
MDPI AG