Evidence map›Paper›PMID 35061008›Full record

ArticleThe Journal of cell biology2022

Atg39 links and deforms the outer and inner nuclear membranes in selective autophagy of the nucleus.

Keisuke Mochida, Toshifumi Otani, Yuto Katsumata, Hiromi Kirisako, Chika Kakuta, Tetsuya Kotani, Hitoshi Nakatogawa

Open access · bronzeAbstract 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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.3field-weighted citation impact, top 4% 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

27 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Atg39-dependent nucleophagy and Atg40-dependent ER-phagy require the Apq12/Brr6/Brl1 complex.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Multifunctional Roles of Autophagy in Fungi.Journal of fungi (Basel, Switzerland) · 2026
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Nuclear envelope budding: Getting large macromolecular complexes out of the nucleus.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024
    Article
  15. Methods to Monitor Nucleophagy in Yeast.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. 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

7 authors at 1 institution in 1 country.

Keisuke MochidaSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.ORCID 0000-0003-2090-0543
Toshifumi OtaniSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Yuto KatsumataSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Hiromi KirisakoSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Chika KakutaSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Tetsuya KotaniSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Hitoshi NakatogawaSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.ORCID 0000-0002-5828-0741
Tokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In selective autophagy of the nucleus (hereafter nucleophagy), nucleus-derived double-membrane vesicles (NDVs) are formed, sequestered within autophagosomes, and delivered to lysosomes or vacuoles for degradation. In Saccharomyces cerevisiae, the nuclear envelope (NE) protein Atg39 acts as a nucleophagy receptor, which interacts with Atg8 to target NDVs to the forming autophagosomal membranes. In this study, we revealed that Atg39 is anchored to the outer nuclear membrane via its transmembrane domain and also associated with the inner nuclear membrane via membrane-binding amphipathic helices (APHs) in its perinuclear space region, thereby linking these membranes. We also revealed that autophagosome formation-coupled Atg39 crowding causes the NE to protrude toward the cytoplasm, and the tips of the protrusions are pinched off to generate NDVs. The APHs of Atg39 are crucial for Atg39 crowding in the NE and subsequent NE protrusion. These findings suggest that the nucleophagy receptor Atg39 plays pivotal roles in NE deformation during the generation of NDVs to be degraded by nucleophagy.

Indexed as

AutophagyAutophagy-Related ProteinsChromosomes, FungalNuclear EnvelopeReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAtg39 protein, S cerevisiaeAutophagy-Related ProteinsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae Proteins

Identifiers

PMID35061008
PMCPMC8789198
OpenAlexW4225644735

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.