Evidence map›Paper›PMID 25484098›Full record

ArticleAutophagy2014

PHF23 (plant homeodomain finger protein 23) negatively regulates cell autophagy by promoting ubiquitination and degradation of E3 ligase LRSAM1.

Zhenda Wang, Jia Hu, Ge Li, Liujing Qu, Qihua He, Yaxin Lou, Quansheng Song, Dalong Ma, Yingyu Chen

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Oncogenic role of PHF23 in gastric cancer progression.Functional & integrative genomics · 2026
    Article
  4. Article
  5. Article
  6. Structure, function, and pathology of PHF23.Frontiers in cell and developmental biology · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Writing, erasing and reading histone lysine methylations.Experimental & molecular medicine · 2017
    Review
  18. Review
  19. Article
  20. 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

9 authors at 2 institutions in 4 countries.

Zhenda Wanga Key Laboratory of Medical Immunology; Ministry of Health ; Peking University Health Science Center ; Beijing , China.
Jia Hu
Ge Li
Liujing Qu
Qihua He
Yaxin Lou
Quansheng Song
Dalong Ma
Yingyu Chen
Peking University · CNState Key Laboratory of Medical Immunology

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is a multistep process that involves the degradation and digestion of intracellular components by the lysosome. It has been proved that many core autophagy-related molecules participate in this event. However, new component proteins that regulate autophagy are still being discovered. At present, we report PHF23 (PHD finger protein 23) with a PHD-like zinc finger domain that can negatively regulate autophagy. Data from experiments indicated that the overexpression of PHF23 impaired autophagy, as characterized by decreased levels of LC3B-II and weakened degradation of endogenous and exogenous autophagic substrates. Conversely, knockdown of PHF23 resulted in opposite effects. Molecular mechanism studies suggested that PHF23 interacts with LRSAM1, which is an E3 ligase key for ubiquitin-dependent autophagy against invading bacteria. PHF23 promotes the ubiquitination and proteasome degradation of LRSAM1. We also show that the PHD finger of PHF23 is a functional domain needed for the interaction with LRSAM1. Altogether, our results indicate that PHF23 is a negative regulator associated in autophagy via the LRSAM1 signaling pathway. The physical and functional connection between the PHF23 and LRSAM1 needs further investigation.

Indexed as

AutophagyCell LineHomeodomain ProteinsHumansLysosomesSignal TransductionUbiquitinUbiquitinationUbiquitin-Protein LigasesHomeodomain ProteinsLRSAM1 protein, humanPHF23 protein, humanUbiquitinUbiquitin-Protein LigasesAML, acute myeloid leukemiaATG, autophagy-relatedautophagyBafA1, bafilomycin A1CALCOCO2, calcium binding and coiled-coil domain 2CQ, chloroquineEBSS, Earle's balanced salt solutionFBS, fetal bovine serumGFP, green fluorescent proteinGST, glutathione S-transferaseIP, immunoprecipitationLRSAM1LRSAM1, leucine rich repeat and sterile α motif containing 1MAP1LC3B/LC3Bmicrotubule-associated protein 1 light chain 3 βPHD domainPHD, plant homeodomainPHF23PHF23, PHD finger protein 23PIK3C3, phosphatidylinositol 3-kinase, catalytic subunit type 3SQSTM1, sequestosome 1Three-MA, 3-methyladenineubiquitination

Identifiers

PMID25484098
PMCPMC4502667
OpenAlexW2049686095

What OpenQuestion holds

Textmetadata
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.