Evidence map›Paper›PMID 20154084›Full record

ArticleThe Journal of biological chemistry2010

Roles of the lipid-binding motifs of Atg18 and Atg21 in the cytoplasm to vacuole targeting pathway and autophagy.

Usha Nair, Yang Cao, Zhiping Xie, Daniel J Klionsky

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
8.3field-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

78 citing papers in PubMed, 127 citations in OpenAlex.

  1. Article
  2. Functional Homology of WIPI4 and Atg18 EnablesInternational journal of molecular sciences · 2026
    Article
  3. Review
  4. Article
  5. NADCells · 2025
    Review
  6. mSphere · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Degradation Mechanism of Autophagy-Related Proteins and Research Progress.International journal of molecular sciences · 2022
    Review
  14. MoWhi2 Mediates Mitophagy to Regulate Conidiation and Pathogenesis inInternational journal of molecular sciences · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Small but mighty: Atg8s and Rabs in membrane dynamics during autophagy.Biochimica et biophysica acta. Molecular cell research · 2021
    Review
  20. Review

18 more citing papers are in PubMed but not listed here.

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 at 2 institutions in 2 countries.

Usha NairDepartment of Molecular, Cellular, and Developmental Biology and the Life Sciences Institute, University of Michigan, Ann Arbor, Michigan 48109, USA.
Yang Cao
Zhiping Xie
Daniel J Klionsky
Institut de Biologie Moléculaire et Cellulaire · FRUniversity of Michigan–Ann Arbor · US

Funding

ALTERNATIVE VACUOLAR TARGETING MECHANISMS IN YEASTR01GM053396 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KLIONSKY, DANIEL J. · 1995 to 2018
$12.1M
NIGMS NIH HHS GM53396NIGMS NIH HHS R01 GM053396
6 · The paper itself

Abstract

Atg18 and Atg21 are homologous WD-40 repeat proteins that bind phosphoinositides via a novel conserved Phe-Arg-Arg-Gly motif and function in autophagy-related pathways. Atg18 is required for the cytoplasm to vacuole targeting (Cvt) pathway and autophagy, whereas Atg21 is only required for the Cvt pathway. Currently, the functions of both proteins are poorly understood. Here, we examined the relationship between the phosphatidylinositol 3-phosphate (PtdIns(3)P)-binding abilities of Atg18 and Atg21 and autophagy by expressing variants of these proteins that have mutations in their phosphoinositide-binding motifs. Cells expressing PtdIns(3)P-binding mutants of both these proteins showed highly reduced autophagy. Furthermore, the localization of components of two related ubiquitin-like protein conjugation systems, Atg8 and Atg16, to the phagophore assembly site is affected. Consistent with the aberrant localization of the above Atg proteins, precursor Ape1, a cargo of the Cvt pathway and autophagy, is partially protease-sensitive in starvation conditions. This finding suggests a requirement for the PtdIns(3)P binding capability of Atg18 and Atg21 in efficient completion of the sequestering autophagic vesicles. Finally, using a multiple knock-out strain, we found that Atg18 and Atg21 facilitate the recruitment of Atg8-PE to the site of autophagosome formation and protect it from premature cleavage by Atg4, which represents a key aspect of post-translational autophagy regulation. Taken together, our results suggest that PtdIns(3)P binding by at least Atg18 or Atg21 is required for robust autophagic activity and that the PtdIns(3)P-binding motifs of Atg18 and Atg21 can compensate for one another in the recruitment of Atg components that are dependent on PtdIns(3)P for their phagophore assembly site association.

Indexed as

AutophagyAmino Acid MotifsAutophagy-Related ProteinsCytoplasmEndopeptidasesLipidsMembrane ProteinsMicroscopy, FluorescenceModels, BiologicalMutationPhosphatidylinositol PhosphatesProtein BindingProtein Processing, Post-TranslationalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTwo-Hybrid System TechniquesATG18 protein, S cerevisiaeATG21 protein, S cerevisiaeAutophagy-Related ProteinsEndopeptidasesLipidsMembrane Proteinsphosphatidylinositol 3-phosphatePhosphatidylinositol PhosphatesSaccharomyces cerevisiae Proteins

Identifiers

PMID20154084
PMCPMC2857026
OpenAlexW2023152825

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.