Evidence map›Paper›PMID 39169022›Full record

ArticleNature communications2024

Palmitoylation of ULK1 by ZDHHC13 plays a crucial role in autophagy.

Keisuke Tabata, Kenta Imai, Koki Fukuda, Kentaro Yamamoto, Hayato Kunugi, Toshiharu Fujita, Tatsuya Kaminishi, Christian Tischer, Beate Neumann, Sabine Reither and 4 more

Erratum issuedAbstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. The ATG14: multi-layer autophagy control and an emerging therapeutic target in cancer.Apoptosis : an international journal on programmed cell death · 2026
    Review
  7. Review
  8. Review
  9. SNX-3 confers lysosomal fusion-competence to sustain basal autophagy.Cellular and molecular life sciences : CMLS · 2026
    Article
  10. The Roles of ProteinCancer communications (London, England) · 2026
    Review
  11. Review
  12. Article
  13. Review
  14. The role of autophagy in protozoan infections.Frontiers in cellular and infection microbiology · 2026
    Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors.

Keisuke TabataLaboratory of Intracellular Membrane Dynamics, Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan.ORCID 0000-0001-6776-1689
Kenta ImaiLaboratory of Intracellular Membrane Dynamics, Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan.
Koki FukudaLaboratory of Intracellular Membrane Dynamics, Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan.
Kentaro YamamotoLaboratory of Intracellular Membrane Dynamics, Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan.
Hayato KunugiLaboratory of Intracellular Membrane Dynamics, Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan.
Toshiharu FujitaLaboratory of Intracellular Membrane Dynamics, Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan.
Tatsuya KaminishiDepartment of Genetics, Graduate School of Medicine, Osaka University, Osaka, Japan.ORCID 0000-0001-5056-1074
Christian TischerAdvanced Light Microscopy Facility, EMBL, Heidelberg, Germany.
Beate NeumannAdvanced Light Microscopy Facility, EMBL, Heidelberg, Germany.ORCID 0000-0002-6899-502X
Sabine ReitherAdvanced Light Microscopy Facility, EMBL, Heidelberg, Germany.
Fatima VerissimoAdvanced Light Microscopy Facility, EMBL, Heidelberg, Germany.
Rainer PepperkokAdvanced Light Microscopy Facility, EMBL, Heidelberg, Germany.
Tamotsu YoshimoriLaboratory of Intracellular Membrane Dynamics, Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan. tamyoshi@fbs.osaka-u.ac.jp.ORCID 0000-0001-9787-3788
Maho HamasakiLaboratory of Intracellular Membrane Dynamics, Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan. hamasaki@fbs.osaka-u.ac.jp.ORCID 0000-0002-5646-5136

Funding

MEXT | Japan Society for the Promotion of Science (JSPS) 20K05839MEXT | Japan Society for the Promotion of Science (JSPS) 21K06169MEXT | Japan Society for the Promotion of Science (JSPS) JP15H04371MEXT | Japan Society for the Promotion of Science (JSPS) JP21K06152MEXT | Japan Society for the Promotion of Science (JSPS) JP26251020
6 · The paper itself

Abstract

Autophagy is a highly conserved process from yeast to mammals in which intracellular materials are engulfed by a double-membrane organelle called autophagosome and degrading materials by fusing with the lysosome. The process of autophagy is regulated by sequential recruitment and function of autophagy-related (Atg) proteins. Genetic hierarchical analyses show that the ULK1 complex comprised of ULK1-FIP200-ATG13-ATG101 translocating from the cytosol to autophagosome formation sites as a most upstream ATG factor; this translocation is critical in autophagy initiation. However, how this translocation occurs remains unclear. Here, we show that ULK1 is palmitoylated by palmitoyltransferase ZDHHC13 and translocated to the autophagosome formation site upon autophagy induction. We find that the ULK1 palmitoylation is required for autophagy initiation. Moreover, the ULK1 palmitoylated enhances the phosphorylation of ATG14L, which is required for activating PI3-Kinase and producing phosphatidylinositol 3-phosphate, one of the autophagosome membrane's lipids. Our results reveal how the most upstream ULK1 complex translocates to the autophagosome formation sites during autophagy.

Indexed as

AcyltransferasesAutophagosomesAutophagyAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsIntracellular Signaling Peptides and ProteinsLipoylationAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsHEK293 CellsHumansPhosphatidylinositol PhosphatesPhosphorylationProtein TransportVesicular Transport ProteinsAcyltransferasesAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportATG101 protein, humanATG13 protein, humanATG14 protein, humanAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsIntracellular Signaling Peptides and Proteinsphosphatidylinositol 3-phosphatePhosphatidylinositol PhosphatesRB1CC1 protein, humanULK1 protein, humanVesicular Transport Proteins

Identifiers

PMID39169022
PMCPMC11339336

What OpenQuestion holds

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LicenceCC BY
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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.