Evidence map›Paper›PMID 38902268›Full record

ArticleCell death & disease2024

LAPTM4B counteracts ferroptosis via suppressing the ubiquitin-proteasome degradation of SLC7A11 in non-small cell lung cancer.

Ruyu Yan, Dan Liu, Hongjuan Guo, Minxia Liu, Dongjin Lv, Benny Björkblom, Mingsong Wu, Hongtao Yu, Hao Leng, Bingxiao Lu and 4 more

Abstract read
In one paragraph

Article in Cell death & disease, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Article
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  10. Review
  11. Nanozyme-Driven Ferroptosis-Cuproptosis Interplay in Lung Cancer.International journal of nanomedicine · 2026
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. HMGA2 regulates GPX4 expression and ferroptosis in prostate cancer cells.Biochemical and biophysical research communications · 2024
    Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors.

Ruyu Yan *School of Life Sciences, Anhui Medical University, Hefei, 230032, China.
Dan Liu *School of Life Sciences, Anhui Medical University, Hefei, 230032, China.
Hongjuan GuoSchool of Life Sciences, Anhui Medical University, Hefei, 230032, China.
Minxia LiuSchool of Life Sciences, Anhui Medical University, Hefei, 230032, China.
Dongjin LvDepartment of Clinical Research, The Third Affiliated Hospital of Kunming Medical University (Tumor Hospital of Yunnan Province), Kunming, China.
Benny BjörkblomDepartment of Chemistry, Umeå University, Umeå, 90187, Sweden.
Mingsong WuSchool of Stomatology, Zunyi Medical University, Zunyi, Guizhou, 563000, China.
Hongtao YuSchool of Life Sciences, Anhui Medical University, Hefei, 230032, China.
Hao LengSchool of Life Sciences, Anhui Medical University, Hefei, 230032, China.
Bingxiao LuDepartment of Medical Oncology, The Third Affiliated Hospital of Kunming Medical University (Tumor Hospital of Yunnan Province), Kunming, China.
Yuxiang LiSchool of Life Sciences, Anhui Medical University, Hefei, 230032, China.
Miaomiao GaoSchool of Life Sciences, Anhui Medical University, Hefei, 230032, China.
Tomas BlomFaculty of Medicine, University of Helsinki, Helsinki, 00014, Finland. tomas.blom@orionpharma.com.
Kecheng ZhouSchool of Life Sciences, Anhui Medical University, Hefei, 230032, China. zhoukecheng@ahmu.edu.cn.ORCID 0000-0003-1753-2524

Funding

Academy of Finland (Suomen Akatemia) 303771National Natural Science Foundation of China (National Science Foundation of China) 32100623
6 · The paper itself

Abstract

Non-small cell lung cancer (NSCLC) is a leading cause of cancer-related deaths worldwide, necessitating the identification of novel therapeutic targets. Lysosome Associated Protein Transmembrane 4B (LAPTM4B) is involved in biological processes critical to cancer progression, such as regulation of solute carrier transporter proteins and metabolic pathways, including mTORC1. However, the metabolic processes governed by LAPTM4B and its role in oncogenesis remain unknown. In this study, we conducted unbiased metabolomic screens to uncover the metabolic landscape regulated by LAPTM4B. We observed common metabolic changes in several knockout cell models suggesting of a role for LAPTM4B in suppressing ferroptosis. Through a series of cell-based assays and animal experiments, we demonstrate that LAPTM4B protects tumor cells from erastin-induced ferroptosis both in vitro and in vivo. Mechanistically, LAPTM4B suppresses ferroptosis by inhibiting NEDD4L/ZRANB1 mediated ubiquitination and subsequent proteasomal degradation of the cystine-glutamate antiporter SLC7A11. Furthermore, metabolomic profiling of cancer cells revealed that LAPTM4B knockout leads to a significant enrichment of ferroptosis and associated metabolic alterations. By integrating results from cellular assays, patient tissue samples, an animal model, and cancer databases, this study highlights the clinical relevance of the LAPTM4B-SLC7A11-ferroptosis signaling axis in NSCLC progression and identifies it as a potential target for the development of cancer therapeutics.

Indexed as

Amino Acid Transport System y+Carcinoma, Non-Small-Cell LungFerroptosisLung NeoplasmsProteasome Endopeptidase ComplexUbiquitinAnimalsCell Line, TumorHumansMembrane ProteinsMiceMice, NudeOncogene ProteinsProteolysisUbiquitinationAmino Acid Transport System y+LAPTM4B protein, humanMembrane ProteinsOncogene ProteinsProteasome Endopeptidase ComplexSLC7A11 protein, humanUbiquitin

Identifiers

PMID38902268
PMCPMC11190201

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.