Evidence map›Paper›PMID 37250795›Full record

ArticleiScience2023

A LY6E-PHB1-TRIM21 assembly degrades CD14 protein to mitigate LPS-induced inflammatory response.

Xinyu Zhu, Linxia Zhang, Daobin Feng, Lang Jiang, Peng Sun, Chen Zhao, Xiaoyan Zhang, Jianqing Xu

Open access · goldAbstract read
In one paragraph

Article in iScience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.3field-weighted citation impact, top 19% of its field
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

2 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. 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

8 authors at 3 institutions in 1 country.

Xinyu ZhuShanghai Public Health Clinical Center & Institutes of Biomedical Sciences; Fudan University, Shanghai 201508, P. R. China.
Linxia ZhangShanghai Public Health Clinical Center & Institutes of Biomedical Sciences; Fudan University, Shanghai 201508, P. R. China.
Daobin FengShanghai Public Health Clinical Center & Institutes of Biomedical Sciences; Fudan University, Shanghai 201508, P. R. China.
Lang JiangShanghai Public Health Clinical Center & Institutes of Biomedical Sciences; Fudan University, Shanghai 201508, P. R. China.
Peng SunShanghai Public Health Clinical Center & Institutes of Biomedical Sciences; Fudan University, Shanghai 201508, P. R. China.
Chen ZhaoShanghai Public Health Clinical Center & Institutes of Biomedical Sciences; Fudan University, Shanghai 201508, P. R. China.
Xiaoyan ZhangShanghai Public Health Clinical Center & Institutes of Biomedical Sciences; Fudan University, Shanghai 201508, P. R. China.
Jianqing XuShanghai Public Health Clinical Center & Institutes of Biomedical Sciences; Fudan University, Shanghai 201508, P. R. China.
Shanghai Public Health Clinical Center · CNFudan University · CNZhongshan Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A major theme of host against invading pathogens lies in multiple regulatory nodes that ensure sufficient signals for protection while avoiding excessive signals toward over-inflammation. The TLR4/MD-2/CD14 complex receptor-mediated response to bacterial lipopolysaccharide (LPS) represents a paradigm for understanding the proper control of anti-pathogen innate immunity. In this study, we studied the mechanism by which the glycosylphosphatidylinositol (GPI)-linked LY6E protein constrains LPS response via downregulating CD14. We first showed that LY6E downregulated CD14 via ubiquitin-dependent proteasomal degradation. The subsequent profiling of LY6E protein interactome led to the revelation that the degradation of CD14 by LY6E requires PHB1, which interacts with CD14 in a LY6E-dependent manner. Finally, we identified the PHB1-interacting TRIM21 as the major ubiquitin E3 ligase for the LY6E-mediated ubiquitination of CD14. Together, our study elucidated the molecular basis of LY6E-mediated governance of LPS response, alongside providing new insights to regulatory mechanisms controlling the homeostasis of membrane proteins.

Indexed as

ImmunologyMolecular biology

Identifiers

PMID37250795
PMCPMC10209397
OpenAlexW4378745072

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.