Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding
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 disulfi...
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MDPI AG
2021-10-01
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| author | Motonori Matsusaki Rina Okada Yuya Tanikawa Shingo Kanemura Dai Ito Yuxi Lin Mai Watabe Hiroshi Yamaguchi Tomohide Saio Young-Ho Lee Kenji Inaba Masaki Okumura |
| author_facet | Motonori Matsusaki Rina Okada Yuya Tanikawa Shingo Kanemura Dai Ito Yuxi Lin Mai Watabe Hiroshi Yamaguchi Tomohide Saio Young-Ho Lee Kenji Inaba Masaki Okumura |
| author_sort | Motonori Matsusaki |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T05:42:04Z |
| format | Article |
| id | doaj.art-45ecc0f3a89d47ea96fcc3025c60da76 |
| institution | Directory Open Access Journal |
| issn | 2079-7737 |
| language | English |
| last_indexed | 2024-03-10T05:42:04Z |
| publishDate | 2021-10-01 |
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| series | Biology |
| spelling | doaj.art-45ecc0f3a89d47ea96fcc3025c60da762023-11-22T22:27:31ZengMDPI AGBiology2079-77372021-10-011011111210.3390/biology10111112Functional Interplay between P5 and PDI/ERp72 to Drive Protein FoldingMotonori Matsusaki0Rina Okada1Yuya Tanikawa2Shingo Kanemura3Dai Ito4Yuxi Lin5Mai Watabe6Hiroshi Yamaguchi7Tomohide Saio8Young-Ho Lee9Kenji Inaba10Masaki Okumura11Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3, Aramakiaza Aoba, Aoba-ku, Sendai 980-8578, JapanSchool of Science and Technology, Kwansei Gakuin University, 2-1, Gakuen, Sanda 669-1337, JapanSchool of Science and Technology, Kwansei Gakuin University, 2-1, Gakuen, Sanda 669-1337, JapanFrontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3, Aramakiaza Aoba, Aoba-ku, Sendai 980-8578, JapanDepartment of Brain and Cognitive Science, Daegu Gyeongbuk Institute of Science and Technology, 333, Techno Jungang Daero, Daegu 42988, KoreaResearch Center for Bioconvergence Analysis, Korea Basic Science Institute, 162, Yeongudanji-ro, Ochang-eup, Cheongwon-gu, Cheongju-si 28119, KoreaFrontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3, Aramakiaza Aoba, Aoba-ku, Sendai 980-8578, JapanSchool of Science and Technology, Kwansei Gakuin University, 2-1, Gakuen, Sanda 669-1337, JapanInstitute of Advanced Medical Sciences, Tokushima University, 3-18-15, Kuramoto-cho, Tokushima 770-8503, JapanResearch Center for Bioconvergence Analysis, Korea Basic Science Institute, 162, Yeongudanji-ro, Ochang-eup, Cheongwon-gu, Cheongju-si 28119, KoreaInstitute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai 980-8577, JapanFrontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3, Aramakiaza Aoba, Aoba-ku, Sendai 980-8578, JapanP5 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.https://www.mdpi.com/2079-7737/10/11/1112protein disulfide isomerase familydisulfide bondendoplasmic reticulumoxidative foldingmolecular chaperoneprotein-protein interaction |
| spellingShingle | Motonori Matsusaki Rina Okada Yuya Tanikawa Shingo Kanemura Dai Ito Yuxi Lin Mai Watabe Hiroshi Yamaguchi Tomohide Saio Young-Ho Lee Kenji Inaba Masaki Okumura Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding Biology protein disulfide isomerase family disulfide bond endoplasmic reticulum oxidative folding molecular chaperone protein-protein interaction |
| title | Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding |
| title_full | Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding |
| title_fullStr | Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding |
| title_full_unstemmed | Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding |
| title_short | Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding |
| title_sort | functional interplay between p5 and pdi erp72 to drive protein folding |
| topic | protein disulfide isomerase family disulfide bond endoplasmic reticulum oxidative folding molecular chaperone protein-protein interaction |
| url | https://www.mdpi.com/2079-7737/10/11/1112 |
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