Evidence map›Paper›PMID 39472561›Full record

ArticleNature communications2024

AAA+ ATPase chaperone p97/VCP

Fumika Koyano, Koji Yamano, Tomoyuki Hoshina, Hidetaka Kosako, Yukio Fujiki, Keiji Tanaka, Noriyuki Matsuda

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. 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.

Fumika KoyanoDepartment of Biomolecular Pathogenesis, Medical Research Institute, Tokyo Medical and Dental University (TMDU) (Medical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo), 1-5-45 Yushima, Bunkyo-ku, Tokyo, 113-8510, Japan. koyano-fm.biom@tmd.ac.jp.ORCID 0000-0003-4298-0492
Koji YamanoDepartment of Biomolecular Pathogenesis, Medical Research Institute, Tokyo Medical and Dental University (TMDU) (Medical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo), 1-5-45 Yushima, Bunkyo-ku, Tokyo, 113-8510, Japan.
Tomoyuki HoshinaDepartment of Biomolecular Pathogenesis, Medical Research Institute, Tokyo Medical and Dental University (TMDU) (Medical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo), 1-5-45 Yushima, Bunkyo-ku, Tokyo, 113-8510, Japan.
Hidetaka KosakoDivision of Cell Signaling, Fujii Memorial Institute of Medical Sciences, Institute of Advanced Medical Sciences, Tokushima University, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan.ORCID 0000-0003-3228-6368
Yukio FujikiMedical Institute of Bioregulation, Institute of Rheological Functions of Food-Kyushu University Collaboration Program, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, 812-8582, Japan.ORCID 0000-0002-8138-6376
Keiji TanakaLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, 2-1-6 Kamikitazawa, Setagaya, Tokyo, 156-8506, Japan.
Noriyuki MatsudaDepartment of Biomolecular Pathogenesis, Medical Research Institute, Tokyo Medical and Dental University (TMDU) (Medical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo), 1-5-45 Yushima, Bunkyo-ku, Tokyo, 113-8510, Japan. nr-matsuda.biom@tmd.ac.jp.ORCID 0000-0001-8199-952X

Funding

Japan Agency for Medical Research and Development (AMED) JP23gm1410004MEXT | Japan Society for the Promotion of Science (JSPS) JP15K19037, JP18K14708, JP21K06161MEXT | Japan Society for the Promotion of Science (JSPS) JP18H05500, JP16K18545, JP18K06237MEXT | Japan Society for the Promotion of Science (JSPS) JP19H05712MEXT | Japan Society for the Promotion of Science (JSPS) JP26000014, JP19H00997MEXT | Japan Society for the Promotion of Science (JSPS) JP26116007, JP15K21743, JP17H03675
6 · The paper itself

Abstract

Peroxisomes are organelles that are central to lipid metabolism and chemical detoxification. Despite advances in our understanding of peroxisome biogenesis, the mechanisms maintaining peroxisomal membrane proteins remain to be fully elucidated. We show here that mammalian FAF2/UBXD8, a membrane-associated cofactor of p97/VCP, maintains peroxisomal homeostasis by modulating the turnover of peroxisomal membrane proteins such as PMP70. In FAF2-deficient cells, PMP70 accumulation recruits the autophagy adaptor OPTN (Optineurin) to peroxisomes and promotes their autophagic clearance (pexophagy). Pexophagy is also induced by p97/VCP inhibition. FAF2 functions together with p97/VCP to negatively regulate pexophagy rather than as a factor for peroxisome biogenesis. Our results strongly suggest that p97/VCP

Indexed as

PeroxisomesValosin Containing ProteinAdenosine TriphosphatasesAnimalsAutophagyCell Cycle ProteinsHEK293 CellsHeLa CellsHumansMacroautophagyMembrane ProteinsMembrane Transport ProteinsMiceMolecular ChaperonesAdenosine TriphosphatasesCell Cycle ProteinsMembrane ProteinsMembrane Transport ProteinsMolecular ChaperonesOPTN protein, humanValosin Containing ProteinVCP protein, human

Identifiers

PMID39472561
PMCPMC11522385

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.