Evidence map›Paper›PMID 31222192›Full record

ArticleNature chemical biology2019

The cholesterol transfer protein GRAMD1A regulates autophagosome biogenesis.

Luca Laraia, Alexandra Friese, Dale P Corkery, Georgios Konstantinidis, Nelli Erwin, Walter Hofer, Hacer Karatas, Laura Klewer, Andreas Brockmeyer, Malte Metz and 11 more

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed, 3 pooled it
8.5field-weighted citation impact, top 2% 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

52 citing papers in PubMed, 3 syntheses or guidelines pooled it, 91 citations in OpenAlex.

  1. Pooled it
  2. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
    Pooled it
  3. Guideline
  4. Article
  5. Design and structural basis of selective nonsteroidal inhibitors of aster cholesterol trafficking.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The multimodal transcriptional response of denervated skeletal muscle involves regulation ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

21 authors at 5 institutions in 3 countries.

Luca LaraiaDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID http://orcid.org/0000-0001-6692-3412
Alexandra FrieseDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Dale P CorkeryChemical Genomics Centre of the Max Planck Society, Dortmund, Germany.ORCID http://orcid.org/0000-0001-7930-0134
Georgios KonstantinidisChemical Genomics Centre of the Max Planck Society, Dortmund, Germany.
Nelli ErwinFaculty of Chemistry and Chemical Biology, Technical University Dortmund, Dortmund, Germany.
Walter HoferDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Hacer KaratasDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Laura KlewerChemical Genomics Centre of the Max Planck Society, Dortmund, Germany.
Andreas BrockmeyerDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Malte MetzDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Beate SchölermannDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Mridula DwivediFaculty of Chemistry and Chemical Biology, Technical University Dortmund, Dortmund, Germany.
Lei LiFaculty of Chemistry and Chemical Biology, Technical University Dortmund, Dortmund, Germany.
Pablo Rios-MunozCentre for Biological Signalling Studies (BIOSS), University of Freiburg, Freiburg, Germany.
Maja KöhnCentre for Biological Signalling Studies (BIOSS), University of Freiburg, Freiburg, Germany.
Roland WinterFaculty of Chemistry and Chemical Biology, Technical University Dortmund, Dortmund, Germany.
Ingrid R VetterDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Slava ZieglerDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Petra JanningDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Yao-Wen WuChemical Genomics Centre of the Max Planck Society, Dortmund, Germany. yaowen.wu@umu.se.ORCID http://orcid.org/0000-0002-2573-8736
Herbert WaldmannDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany. herbert.waldmann@mpi-dortmund.mpg.de.ORCID http://orcid.org/0000-0002-9606-7247
Max Planck Institute of Molecular Physiology · DETU Dortmund University · DEMax Planck Society · DEUniversity of Freiburg · DEChemical Genomics Centre · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy mediates the degradation of damaged proteins, organelles and pathogens, and plays a key role in health and disease. Thus, the identification of new mechanisms involved in the regulation of autophagy is of major interest. In particular, little is known about the role of lipids and lipid-binding proteins in the early steps of autophagosome biogenesis. Using target-agnostic, high-content, image-based identification of indicative phenotypic changes induced by small molecules, we have identified autogramins as a new class of autophagy inhibitor. Autogramins selectively target the recently discovered cholesterol transfer protein GRAM domain-containing protein 1A (GRAMD1A, which had not previously been implicated in autophagy), and directly compete with cholesterol binding to the GRAMD1A StART domain. GRAMD1A accumulates at sites of autophagosome initiation, affects cholesterol distribution in response to starvation and is required for autophagosome biogenesis. These findings identify a new biological function of GRAMD1A and a new role for cholesterol in autophagy.

Indexed as

AutophagosomesAutophagyHumansMembrane ProteinsModels, MolecularSmall Molecule LibrariesTumor Cells, CulturedGRAMD1A protein, humanMembrane ProteinsSmall Molecule Libraries

Identifiers

PMID31222192
OpenAlexW2950635058

What OpenQuestion holds

Textmetadata
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.