Proteomic analysis of ferroptosis pathways reveals a role of CEPT1 in suppressing ferroptosis

Xiaoguang Liu; Zhen Chen; Yuelong Yan; Fereshteh Zandkarimi; Litong Nie; Qidong Li; Amber Horbath; Kellen Olszewski; Lavanya Kondiparthi; Chao Mao; Hyemin Lee; Li Zhuang; Masha Poyurovsky; Brent R. Stockwell; Junjie Chen; Boyi Gan

doi:10.1093/procel/pwae004

Proteomic analysis of ferroptosis pathways reveals a role of CEPT1 in suppressing ferroptosis

Xiaoguang Liu, Zhen Chen, Yuelong Yan, Fereshteh Zandkarimi, Litong Nie, Qidong Li, Amber Horbath, Kellen Olszewski, Lavanya Kondiparthi, Chao Mao, Hyemin Lee, Li Zhuang, Masha Poyurovsky, Brent R. Stockwell, Junjie Chen, Boyi Gan

Princeton Branch of the Ludwig Institute for Cancer Research

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

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.

Original language	English (US)
Pages (from-to)	686-703
Number of pages	18
Journal	Protein and Cell
Volume	15
Issue number	9
DOIs	https://doi.org/10.1093/procel/pwae004
State	Published - Sep 1 2024

All Science Journal Classification (ASJC) codes

Biotechnology
Biochemistry
Drug Discovery
Cell Biology

Keywords

CEPT1
LPCAT3
ferroptosis
proteomics

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10.1093/procel/pwae004

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title = "Proteomic analysis of ferroptosis pathways reveals a role of CEPT1 in suppressing ferroptosis",

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.",

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author = "Xiaoguang Liu and Zhen Chen and Yuelong Yan and Fereshteh Zandkarimi and Litong Nie and Qidong Li and Amber Horbath and Kellen Olszewski and Lavanya Kondiparthi and Chao Mao and Hyemin Lee and Li Zhuang and Masha Poyurovsky and Stockwell, {Brent R.} and Junjie Chen and Boyi Gan",

note = "Publisher Copyright: {\textcopyright} 2024 The Author(s). Published by Oxford University Press on behalf of Higher Education Press.",

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doi = "10.1093/procel/pwae004",

language = "English (US)",

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T1 - Proteomic analysis of ferroptosis pathways reveals a role of CEPT1 in suppressing ferroptosis

AU - Liu, Xiaoguang

AU - Chen, Zhen

AU - Yan, Yuelong

AU - Zandkarimi, Fereshteh

AU - Nie, Litong

AU - Li, Qidong

AU - Horbath, Amber

AU - Olszewski, Kellen

AU - Kondiparthi, Lavanya

AU - Mao, Chao

AU - Lee, Hyemin

AU - Zhuang, Li

AU - Poyurovsky, Masha

AU - Stockwell, Brent R.

AU - Chen, Junjie

AU - Gan, Boyi

PY - 2024/9/1

Y1 - 2024/9/1

N2 - 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.

AB - 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.

KW - CEPT1

KW - LPCAT3

KW - ferroptosis

KW - proteomics

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DO - 10.1093/procel/pwae004

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AN - SCOPUS:85202960208

SN - 1674-800X

VL - 15

SP - 686

EP - 703

JO - Protein and Cell

JF - Protein and Cell

IS - 9

ER -

Proteomic analysis of ferroptosis pathways reveals a role of CEPT1 in suppressing ferroptosis

Abstract

All Science Journal Classification (ASJC) codes

Keywords

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