期刊
JOURNAL OF CELL BIOLOGY
卷 202, 期 6, 页码 861-874出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201303027
关键词
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类别
资金
- Ministry of Education, Culture, Sports, Science and Technology [19G0314, 19058008, 25102008, 24249002]
- New Energy and Industrial Technology Development Organization
- Japan Society for the Promotion of Science
- [22020039]
- Grants-in-Aid for Scientific Research [25102001, 19058008, 25102008] Funding Source: KAKEN
Ero1-alpha and endoplasmic reticulum (ER) oxidoreductases of the protein disulfide isomerase (PDI) family promote the efficient introduction of disulfide bonds into nascent polypeptides in the ER. However, the hierarchy of electron transfer among these oxidoreductases is poorly understood. In this paper, Ero1-alpha-associated oxidoreductases were identified by proteomic analysis and further confirmed by surface plasmon resonance. Ero1-alpha and PDI were found to constitute a regulatory hub, whereby PDI induced conformational flexibility in an Ero1-alpha shuttle cysteine (Cys99) facilitated intramolecular electron transfer to the active site. In isolation, Ero1-alpha also oxidized ERp46, ERp57, and P5; however, kinetic measurements and redox equilibrium analysis revealed that PDI preferentially oxidized other oxidoreductases. PDI accepted electrons from the other oxidoreductases via its a' domain, bypassing the a domain, which serves as the electron acceptor from reduced glutathione. These observations provide an integrated picture of the hierarchy of cooperative redox interactions among ER oxidoreductases in mammalian cells.
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