Evidence map›Paper›PMID 42032884›Full record

ArticleFEBS letters2026

The ubiquitin ligase RNF115 is required for the clearance of damaged lysosomes.

Sae Nakanaga, Toshiki Takahashi, Akiko Kuma, Hiroyuki Kawahara

Abstract read
In one paragraph

Article in FEBS letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

4 authors.

Sae NakanagaLaboratory of Cell Biology and Biochemistry, Department of Biological Sciences, Tokyo Metropolitan University, Japan.
Toshiki TakahashiLaboratory of Cell Biology and Biochemistry, Department of Biological Sciences, Tokyo Metropolitan University, Japan.
Akiko KumaGraduate School of Medicine, Division of Health Sciences, The University of Osaka, Japan.
Hiroyuki KawaharaLaboratory of Cell Biology and Biochemistry, Department of Biological Sciences, Tokyo Metropolitan University, Japan.ORCID https://orcid.org/0000-0001-8506-9012

Funding

Research fund for future infectious disease measures and Advanced Research from Tokyo Metropolitan Government R4-1Takeda Science FoundationThe Japan Society for the Promotion of Science (JSPS) KAKENHI 20H00457The Japan Society for the Promotion of Science (JSPS) KAKENHI 24H01905The Japan Society for the Promotion of Science (JSPS) KAKENHI 24K01978
6 · The paper itself

Abstract

Lysosomes play a critical role in the quality control of cellular organelles. However, lysosomal membranes can be damaged under a variety of conditions, leading to the onset of various diseases. Damaged lysosomes are selectively cleared via a ubiquitin-dependent mechanism, but the molecular mechanisms underlying this process have not been adequately elucidated. In this study, we found that RNF115 is a lysosomal damage-responsive ubiquitin ligase that undergoes massive translocation from the cytosol to the p62/SQSTM1-positive puncta around ruptured lysosomes. In accordance with the changes in its distribution, the depletion of RNF115 delayed the removal of Gal3 from damaged lysosomes during the restoration process following lysosomal damage. These observations suggest that RNF115 is responsible for the clearance of damaged lysosomes.

Indexed as

LysosomesUbiquitin-Protein LigasesAnimalsAutophagyCytosolHeLa CellsHumansProtein TransportSequestosome-1 ProteinSequestosome-1 ProteinUbiquitin-Protein LigasesautophagyBAG6E3 ubiquitin ligaselysophagylysosomal membrane damagelysosomeRNF115

Identifiers

PMID42032884
PMCPMC13358411

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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.