Evidence map›Paper›PMID 37191320›Full record

ArticleAutophagy2023

Hva22, a REEP family protein in fission yeast, promotes reticulophagy in collaboration with a receptor protein.

Tomoyuki Fukuda, Tetsu Saigusa, Kentaro Furukawa, Keiichi Inoue, Shun-Ichi Yamashita, Tomotake Kanki

Open access · greenAbstract read
In one paragraph

Article in Autophagy, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Core principles of autophagy initiation mechanisms.Nature structural & molecular biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Frontiers in plant science · 2023
    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

6 authors at 1 institution in 1 country.

Tomoyuki FukudaDepartment of Cellular Physiology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.ORCID 0000-0003-2069-7127
Tetsu SaigusaDepartment of Cellular Physiology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.
Kentaro FurukawaDepartment of Cellular Physiology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.ORCID 0000-0002-1551-1538
Keiichi InoueDepartment of Cellular Physiology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.ORCID 0000-0002-7101-486X
Shun-Ichi YamashitaDepartment of Cellular Physiology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.ORCID 0000-0001-8892-0765
Tomotake KankiDepartment of Cellular Physiology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.ORCID 0000-0001-9646-5379
Niigata University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endoplasmic reticulum (ER) undergoes selective autophagy called reticulophagy or ER-phagy. Multiple reticulon- and receptor expression enhancing protein (REEP)-like ER-shaping proteins, including budding yeast Atg40, serve as reticulophagy receptors that stabilize the phagophore on the ER by interacting with phagophore-conjugated Atg8. Additionally, they facilitate phagophore engulfment of the ER by remodeling ER morphology. We reveal that Hva22, a REEP family protein in fission yeast, promotes reticulophagy without Atg8-binding capacity. The role of Hva22 in reticulophagy can be replaced by expressing Atg40 independently of its Atg8-binding ability. Conversely, adding an Atg8-binding sequence to Hva22 enables it to substitute for Atg40 in budding yeast. Thus, the phagophore-stabilizing and ER-shaping activities, both of which Atg40 solely contains, are divided between two separate factors, receptors and Hva22, respectively, in fission yeast.

Indexed as

AutophagySchizosaccharomycesAutophagosomesCarrier ProteinsEndoplasmic ReticulumCarrier ProteinsAtg40autophagyendoplasmic reticulum (ER)ER-phagyER-shapingHva22REEPreticulonreticulophagyyeasts

Identifiers

PMID37191320
PMCPMC10472877
OpenAlexW4376641236

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.