Evidence map›Paper›PMID 32453403›Full record

ArticleThe Journal of cell biology2020

TORC1 inactivation stimulates autophagy of nucleoporin and nuclear pore complexes.

Yui Tomioka, Tetsuya Kotani, Hiromi Kirisako, Yu Oikawa, Yayoi Kimura, Hisashi Hirano, Yoshinori Ohsumi, Hitoshi Nakatogawa

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

44 citing papers in PubMed, 70 citations in OpenAlex.

  1. Multifunctional Roles of Autophagy in Fungi.Journal of fungi (Basel, Switzerland) · 2026
    Review
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  16. Methods to Monitor Nucleophagy in Yeast.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  17. Article
  18. Article
  19. A Yeast Mitotic Tale for the Nucleus and the Vacuoles to Embrace.International journal of molecular sciences · 2023
    Review
  20. Mec1 regulates PAS recruitment of Atg13 via direct binding with Atg13 during glucose starvation-induced autophagy.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Yui TomiokaSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Tetsuya KotaniSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Hiromi KirisakoSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Yu OikawaInstitute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.
Yayoi KimuraAdvanced Medical Research Center, Yokohama City University, Yokohama, Japan.
Hisashi HiranoAdvanced Medical Research Center, Yokohama City University, Yokohama, Japan.
Yoshinori OhsumiInstitute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.
Hitoshi NakatogawaSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Tokyo Institute of Technology · JPYokohama City University Medical Center · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanisms underlying turnover of the nuclear pore complex (NPC) and the component nucleoporins (Nups) are still poorly understood. In this study, we found that the budding yeast Saccharomyces cerevisiae triggers NPC degradation by autophagy upon the inactivation of Tor kinase complex 1. This degradation largely depends on the selective autophagy-specific factor Atg11 and the autophagy receptor-binding ability of Atg8, suggesting that the NPC is degraded via receptor-dependent selective autophagy. Immunoelectron microscopy revealed that NPCs embedded in nuclear envelope-derived double-membrane vesicles are sequestered within autophagosomes. At least two pathways are involved in NPC degradation: Atg39-dependent nucleophagy (selective autophagy of the nucleus) and a pathway involving an unknown receptor. In addition, we found the interaction between Nup159 and Atg8 via the Atg8-family interacting motif is important for degradation of this nucleoporin not assembled into the NPC. Thus, this study provides the first evidence for autophagic degradation of the NPC and Nups, which we term "NPC-phagy" and "nucleoporinophagy."

Indexed as

AutophagosomesAutophagyAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsGene Expression Regulation, FungalMechanistic Target of Rapamycin Complex 1Microscopy, ImmunoelectronNuclear PoreNuclear Pore Complex ProteinsProtein BindingProtein Kinase InhibitorsProteolysisReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionAtg11 protein, S cerevisiaeAtg39 protein, S cerevisiaeATG8 protein, S cerevisiaeAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsMechanistic Target of Rapamycin Complex 1Nuclear Pore Complex ProteinsNUP159 protein, S cerevisiaeProtein Kinase InhibitorsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae ProteinsSirolimusVesicular Transport Proteins

Identifiers

PMID32453403
PMCPMC7337488
OpenAlexW3030784388

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.