Evidence map›Paper›PMID 38009729›Full record

ArticleAutophagy2024

TRIM22 facilitates autophagosome-lysosome fusion by mediating the association of GABARAPs and PLEKHM1.

Hansol Heo, Hyungsun Park, Myung Shin Lee, Jongyoon Kim, Juyeong Kim, Soon-Young Jung, Sun Kyeon Kim, Seongju Lee, Jaerak Chang

Open access · hybridAbstract read
In one paragraph

Article in Autophagy, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

25 citing papers in PubMed, 26 citations in OpenAlex.

  1. Ubiquitination-Related Diagnostic Biomarkers for Diabetic Nephropathy: Insights From Multiomic Analysis, Drug Docking, and Experimental Validation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
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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 1 country.

Hansol HeoDepartment of Biomedical Sciences, Ajou University School of Medicine, Suwon, Republic of Korea.
Hyungsun ParkDepartment of Anatomy, College of Medicine, and Program in Biomedical Science & Engineering, Inha University, Incheon, Republic of Korea.
Myung Shin LeeDepartment of Biomedical Sciences, Ajou University School of Medicine, Suwon, Republic of Korea.
Jongyoon KimDepartment of Anatomy, College of Medicine, and Program in Biomedical Science & Engineering, Inha University, Incheon, Republic of Korea.
Juyeong KimDepartment of Biomedical Sciences, Ajou University School of Medicine, Suwon, Republic of Korea.
Soon-Young JungDepartment of Biomedical Sciences, Ajou University School of Medicine, Suwon, Republic of Korea.
Sun Kyeon KimDepartment of Anatomy, College of Medicine, and Program in Biomedical Science & Engineering, Inha University, Incheon, Republic of Korea.
Seongju LeeDepartment of Anatomy, College of Medicine, and Program in Biomedical Science & Engineering, Inha University, Incheon, Republic of Korea.ORCID 0000-0001-8962-5645
Jaerak ChangDepartment of Biomedical Sciences, Ajou University School of Medicine, Suwon, Republic of Korea.ORCID 0000-0003-1732-2076
Inha University · KRAjou University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tripartite motif (TRIM) proteins are a large family of E3 ubiquitin ligases implicated in antiviral defense systems, tumorigenesis, and protein quality control. TRIM proteins contribute to protein quality control by regulating the ubiquitin-proteasome system, endoplasmic reticulum-associated degradation, and macroautophagy/autophagy. However, the detailed mechanisms through which various TRIM proteins regulate downstream events have not yet been fully elucidated. Herein, we identified a novel function of TRIM22 in the regulation of autophagy. TRIM22 promotes autophagosome-lysosome fusion by mediating the association of GABARAP family proteins with PLEKHM1, thereby inducing the autophagic clearance of protein aggregates, independent of its E3 ubiquitin ligase activity. Furthermore, a TRIM22 variant associated with early-onset familial Alzheimer disease interferes with autophagosome-lysosome fusion and autophagic clearance. These findings suggest TRIM22 as a critical autophagic regulator that orchestrates autophagosome-lysosome fusion by scaffolding autophagy-related proteins, thus representing a potential therapeutic target in neurodegenerative diseases.

Indexed as

Adaptor Proteins, Signal TransducingAutophagosomesAutophagyLysosomesMembrane FusionTripartite Motif ProteinsAlzheimer DiseaseAnimalsApoptosis Regulatory ProteinsAutophagy-Related ProteinsHEK293 CellsHumansMicrotubule-Associated ProteinsMinor Histocompatibility AntigensProtein BindingRepressor ProteinsAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsAutophagy-Related ProteinsGABARAP protein, humanMicrotubule-Associated ProteinsMinor Histocompatibility AntigensPLEKHM1 protein, humanRepressor ProteinsTRIM22 protein, humanTripartite Motif ProteinsAlzheimer diseaseautophagosome-lysosome fusionautophagyPLEKHM1TRIM22

Identifiers

PMID38009729
PMCPMC11135824
OpenAlexW4389057185

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.