Evidence map›Paper›PMID 39875384›Full record

ArticleNature communications2025

Activation of lysophagy by a TBK1-SCF

Na Yeon Park, Doo Sin Jo, Jae-Yoon Yang, Ji-Eun Bae, Joon Bum Kim, Yong Hwan Kim, Seong Hyun Kim, Pansoo Kim, Dong-Seok Lee, Tamotsu Yoshimori and 3 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Lysosomal homeostasis at the crossroads of neurodegeneration.The Journal of clinical investigation · 2026
    Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. The TBK1-SCFAutophagy · 2025
    Article
  11. Review
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

13 authors.

Na Yeon ParkSchool of Life Sciences, BK21 FOUR KNU Creative BioRearch Group, Kyungpook National University, Daegu, South Korea.ORCID http://orcid.org/0009-0004-3552-0062
Doo Sin JoORGASIS Corp. 260, Suwon, South Korea.
Jae-Yoon YangSchool of Life Sciences, BK21 FOUR KNU Creative BioRearch Group, Kyungpook National University, Daegu, South Korea.
Ji-Eun BaeOrganelle Institute, Kyungpook National University, Daegu, South Korea.ORCID http://orcid.org/0009-0000-3472-5112
Joon Bum KimSchool of Life Sciences, BK21 FOUR KNU Creative BioRearch Group, Kyungpook National University, Daegu, South Korea.
Yong Hwan KimSchool of Life Sciences, BK21 FOUR KNU Creative BioRearch Group, Kyungpook National University, Daegu, South Korea.
Seong Hyun KimSchool of Life Sciences, BK21 FOUR KNU Creative BioRearch Group, Kyungpook National University, Daegu, South Korea.
Pansoo KimORGASIS Corp. 260, Suwon, South Korea.
Dong-Seok LeeSchool of Life Sciences, BK21 FOUR KNU Creative BioRearch Group, Kyungpook National University, Daegu, South Korea.ORCID http://orcid.org/0000-0002-7106-1615
Tamotsu YoshimoriDepartment of Genetics, Graduate School of Medicine, Osaka University, Osaka, Japan.
Eun-Kyeong JoDepartment of Microbiology, Chungnam National University College of Medicine, Daejeon, South Korea.ORCID http://orcid.org/0000-0001-7191-0587
Eunbyul YeomSchool of Life Sciences, BK21 FOUR KNU Creative BioRearch Group, Kyungpook National University, Daegu, South Korea. yeb@knu.ac.kr.ORCID http://orcid.org/0009-0001-5926-1227
Dong-Hyung ChoSchool of Life Sciences, BK21 FOUR KNU Creative BioRearch Group, Kyungpook National University, Daegu, South Korea. dhcho@knu.ac.kr.ORCID http://orcid.org/0000-0002-8859-0310

Funding

Korea Institute for Advancement of Technology (KIAT) P0025489National Research Foundation of Korea (NRF) RS-2023-00301914National Research Foundation of Korea (NRF) RS-2024-00338475National Research Foundation of Korea (NRF) RS-2024-00453488National Research Foundation of Korea (NRF) RS-2024-00463344
6 · The paper itself

Abstract

Lysophagy eliminates damaged lysosomes and is crucial to cellular homeostasis; however, its underlying mechanisms are not entirely understood. We screen a ubiquitination-related compound library and determine that the substrate recognition component of the SCF-type E3 ubiquitin ligase complex, SCF

Indexed as

AutophagyF-Box ProteinsIntracellular Signaling Peptides and ProteinsLysosomesMacroautophagyMembrane ProteinsProtein Serine-Threonine KinasesSKP Cullin F-Box Protein LigasesHEK293 CellsHeLa CellsHumansNeoplasm ProteinsPhosphorylationSignal TransductionUbiquitinationF-Box ProteinsIntracellular Signaling Peptides and ProteinsMembrane ProteinsNeoplasm ProteinsProtein Serine-Threonine KinasesSKP Cullin F-Box Protein LigasesTAX1BP1 protein, humanTBK1 protein, human

Identifiers

PMID39875384
PMCPMC11775327

What Socratic 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 Socratic graph.