1. Proteomic analysis of ferroptosis pathways reveals a role of CEPT1 in suppressing ferroptosis.
- Author
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Liu X, Chen Z, Yan Y, Zandkarimi F, Nie L, Li Q, Horbath A, Olszewski K, Kondiparthi L, Mao C, Lee H, Zhuang L, Poyurovsky M, Stockwell BR, Chen J, and Gan B
- Subjects
- Humans, HEK293 Cells, 1-Acylglycerophosphocholine O-Acyltransferase metabolism, 1-Acylglycerophosphocholine O-Acyltransferase genetics, Ferroptosis genetics, Proteomics, Transferases (Other Substituted Phosphate Groups) genetics, Transferases (Other Substituted Phosphate Groups) metabolism
- Abstract
Ferroptosis has been recognized as a unique cell death modality driven by excessive lipid peroxidation and unbalanced cellular metabolism. In this study, we established a protein interaction landscape for ferroptosis pathways through proteomic analyses, and identified choline/ethanolamine phosphotransferase 1 (CEPT1) as a lysophosphatidylcholine acyltransferase 3 (LPCAT3)-interacting protein that regulates LPCAT3 protein stability. In contrast to its known role in promoting phospholipid synthesis, we showed that CEPT1 suppresses ferroptosis potentially by interacting with phospholipases and breaking down certain pro-ferroptotic polyunsaturated fatty acid (PUFA)-containing phospholipids. Together, our study reveals a previously unrecognized role of CEPT1 in suppressing ferroptosis., (© The Author(s) 2024. Published by Oxford University Press on behalf of Higher Education Press.)
- Published
- 2024
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