Evidence map›Paper›PMID 35180289›Full record

ArticleThe Journal of cell biology2022

The core autophagy protein ATG9A controls dynamics of cell protrusions and directed migration.

Daniele Campisi, Laurence Desrues, Kléouforo-Paul Dembélé, Alexandre Mutel, Renaud Parment, Pierrick Gandolfo, Hélène Castel, Fabrice Morin

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Progress on multifunctional transmembrane protein ATG9A.Cell communication and signaling : CCS · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Liver-specific loss ofAutophagy reports · 2025
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. ATG9A supportsMicrobiology spectrum · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

8 authors at 1 institution in 1 country.

Daniele CampisiNormandie University, UNIROUEN, Institut national de la santé et de la recherche médicale U1239, DC2N, Rouen, France.ORCID 0000-0002-5873-9655
Laurence DesruesNormandie University, UNIROUEN, Institut national de la santé et de la recherche médicale U1239, DC2N, Rouen, France.ORCID 0000-0002-6207-8810
Kléouforo-Paul DembéléNormandie University, UNIROUEN, Institut national de la santé et de la recherche médicale U1239, DC2N, Rouen, France.ORCID 0000-0002-6316-3216
Alexandre MutelNormandie University, UNIROUEN, Institut national de la santé et de la recherche médicale U1239, DC2N, Rouen, France.ORCID 0000-0003-2866-7037
Renaud ParmentNormandie University, UNIROUEN, Institut national de la santé et de la recherche médicale U1239, DC2N, Rouen, France.
Pierrick GandolfoNormandie University, UNIROUEN, Institut national de la santé et de la recherche médicale U1239, DC2N, Rouen, France.ORCID 0000-0002-0734-3343
Hélène CastelNormandie University, UNIROUEN, Institut national de la santé et de la recherche médicale U1239, DC2N, Rouen, France.ORCID 0000-0002-8972-5555
Fabrice MorinNormandie University, UNIROUEN, Institut national de la santé et de la recherche médicale U1239, DC2N, Rouen, France.ORCID 0000-0001-6785-1967
Normandie Université · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chemotactic migration is a fundamental cellular behavior relying on the coordinated flux of lipids and cargo proteins toward the leading edge. We found here that the core autophagy protein ATG9A plays a critical role in the chemotactic migration of several human cell lines, including highly invasive glioma cells. Depletion of ATG9A protein altered the formation of large and persistent filamentous actin (F-actin)-rich lamellipodia that normally drive directional migration. Using live-cell TIRF microscopy, we demonstrated that ATG9A-positive vesicles are targeted toward the migration front of polarized cells, where their exocytosis correlates with protrusive activity. Finally, we found that ATG9A was critical for efficient delivery of β1 integrin to the leading edge and normal adhesion dynamics. Collectively, our data uncover a new function for ATG9A protein and indicate that ATG9A-positive vesicles are mobilized during chemotactic stimulation to facilitate expansion of the lamellipodium and its anchorage to the extracellular matrix.

Indexed as

AutophagyCell MovementActinsAutophagy-Related ProteinsCell AdhesionCell Line, TumorCell Surface ExtensionsChemotaxisExocytosisGreen Fluorescent ProteinsHumansIntegrin beta1Membrane GlycoproteinsMembrane ProteinsPseudopodiaReproducibility of ResultsActinsATG9A protein, humanAutophagy-Related ProteinsGreen Fluorescent ProteinsIntegrin beta1Membrane GlycoproteinsMembrane ProteinsPHluorinTGOLN2 protein, humanVesicular Transport Proteins

Identifiers

PMID35180289
PMCPMC8932524
OpenAlexW4212806212

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.