Evidence map›Paper›PMID 33087127›Full record

ReviewJournal of biomedical science2020

Autophagosome formation in relation to the endoplasmic reticulum.

Yo-Hei Yamamoto, Takeshi Noda

Abstract readReview
In one paragraph

Review in Journal of biomedical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Autophagy dark genes: Can we find them with machine learning?Natural sciences (Weinheim, Germany) · 2023
    Article
  10. Review
  11. Article
  12. Article
  13. AmAtg2B-Mediated Lipophagy Regulates Lipolysis of Pupae inInternational journal of molecular sciences · 2023
    Article
  14. Article
  15. Article
  16. The Role of Non-Coding RNAs in Autophagy During Carcinogenesis.Frontiers in cell and developmental biology · 2022
    Review
  17. Role of AMPK in autophagy.Frontiers in physiology · 2022
    Review
  18. Review
  19. Article
  20. A novel variant ofAnnals of translational medicine · 2022
    Article
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

2 authors.

Yo-Hei YamamotoCenter for Frontier Oral Sciences, Graduate School of Dentistry, Osaka University Graduate School, 1-8 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Takeshi NodaCenter for Frontier Oral Sciences, Graduate School of Dentistry, Osaka University Graduate School, 1-8 Yamadaoka, Suita, Osaka, 565-0871, Japan. takenoda@dent.osaka-u.ac.jp.ORCID http://orcid.org/0000-0003-3581-7961

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is a process in which a myriad membrane structures called autophagosomes are formed de novo in a single cell, which deliver the engulfed substrates into lysosomes for degradation. The size of the autophagosomes is relatively uniform in non-selective autophagy and variable in selective autophagy. It has been recently established that autophagosome formation occurs near the endoplasmic reticulum (ER). In this review, we have discussed recent advances in the relationship between autophagosome formation and endoplasmic reticulum. Autophagosome formation occurs near the ER subdomain enriched with phospholipid synthesizing enzymes like phosphatidylinositol synthase (PIS)/CDP-diacylglycerol-inositol 3-phosphatidyltransferase (CDIPT) and choline/ethanolamine phosphotransferase 1 (CEPT1). Autophagy-related protein 2 (Atg2), which is involved in autophagosome formation has a lipid transfer capacity and is proposed to directly transfer the lipid molecules from the ER to form autophagosomes. Vacuole membrane protein 1 (VMP1) and transmembrane protein 41b (TMEM41b) are ER membrane proteins that are associated with the formation of the subdomain. Recently, we have reported that an uncharacterized ER membrane protein possessing the DNAJ domain, called ERdj8/DNAJC16, is associated with the regulation of the size of autophagosomes. The localization of ERdj8/DNAJC16 partially overlaps with the PIS-enriched ER subdomain, thereby implying its association with autophagosome size determination.

Indexed as

AnimalsAutophagosomesAutophagyAutophagy-Related ProteinsEndoplasmic ReticulumHumansAutophagy-Related ProteinsAtg2ATG9AutophagosomeAutophagyCDIPTCOPIIEndoplasmic reticulumERdj8/DNAJC16PISTMEM41bVMP1

Identifiers

PMID33087127
PMCPMC7579975

What OpenQuestion holds

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Registered trials

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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.