Evidence map›Paper›PMID 34817532›Full record

ArticleThe Journal of cell biology2022

PI4P/PS countertransport by ORP10 at ER-endosome membrane contact sites regulates endosome fission.

Asami Kawasaki, Akiko Sakai, Hiroki Nakanishi, Junya Hasegawa, Tomohiko Taguchi, Junko Sasaki, Hiroyuki Arai, Takehiko Sasaki, Michihiro Igarashi, Fubito Nakatsu

Open access · greenAbstract 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 43 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed, 1 pooled it
5.9field-weighted citation impact, top 3% 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

43 citing papers in PubMed, 1 synthesis or guideline pooled it, 71 citations in OpenAlex.

  1. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
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  10. A phosphoinositide-mediated switch of GET pathway receptor dimerization inProceedings of the National Academy of Sciences of the United States of America · 2025
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 1 country.

Asami KawasakiDepartment of Neurochemistry and Molecular Cell Biology, Niigata University School of Medicine and Graduate School of Medical/Dental Sciences, Niigata, Japan.
Akiko SakaiDepartment of Neurochemistry and Molecular Cell Biology, Niigata University School of Medicine and Graduate School of Medical/Dental Sciences, Niigata, Japan.ORCID 0000-0003-3120-0104
Hiroki NakanishiGraduate School of Medicine and Research Center for Biosignal, Akita University, Akita, Japan.
Junya HasegawaDepartment of Biochemical Pathophysiology, Medical Research Institute, Tokyo Medical and Dental University, Tokyo, Japan.ORCID 0000-0003-1216-7468
Tomohiko TaguchiLaboratory of Health Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.ORCID 0000-0003-0464-6370
Junko SasakiDepartment of Biochemical Pathophysiology, Medical Research Institute, Tokyo Medical and Dental University, Tokyo, Japan.
Hiroyuki AraiLaboratory of Health Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Takehiko SasakiGraduate School of Medicine and Research Center for Biosignal, Akita University, Akita, Japan.ORCID 0000-0003-1837-3748
Michihiro IgarashiDepartment of Neurochemistry and Molecular Cell Biology, Niigata University School of Medicine and Graduate School of Medical/Dental Sciences, Niigata, Japan.ORCID 0000-0003-1474-3385
Fubito NakatsuDepartment of Neurochemistry and Molecular Cell Biology, Niigata University School of Medicine and Graduate School of Medical/Dental Sciences, Niigata, Japan.ORCID 0000-0001-9953-3795
Niigata University · JPTokyo Medical and Dental University · JPThe University of Tokyo · JPAkita University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane contact sites (MCSs) serve as a zone for nonvesicular lipid transport by oxysterol-binding protein (OSBP)-related proteins (ORPs). ORPs mediate lipid countertransport, in which two distinct lipids are transported counterdirectionally. How such lipid countertransport controls specific biological functions, however, remains elusive. We report that lipid countertransport by ORP10 at ER-endosome MCSs regulates retrograde membrane trafficking. ORP10, together with ORP9 and VAP, formed ER-endosome MCSs in a phosphatidylinositol 4-phosphate (PI4P)-dependent manner. ORP10 exhibited a lipid exchange activity toward its ligands, PI4P and phosphatidylserine (PS), between liposomes in vitro, and between the ER and endosomes in situ. Cell biological analysis demonstrated that ORP10 supplies a pool of PS from the ER, in exchange for PI4P, to endosomes where the PS-binding protein EHD1 is recruited to facilitate endosome fission. Our study highlights a novel lipid exchange at ER-endosome MCSs as a nonenzymatic PI4P-to-PS conversion mechanism that organizes membrane remodeling during retrograde membrane trafficking.

Indexed as

Endoplasmic ReticulumEndosomesHEK293 CellsHeLa CellsHumansIntracellular MembranesLigandsLiposomesOxysterol Binding ProteinsPhosphatidylinositol PhosphatesPhosphatidylserinesProtein DomainsReceptor, IGF Type 2Receptors, SteroidVesicular Transport ProteinsEHD1 protein, humanLigandsLiposomesOxysterol Binding Proteinsphosphatidylinositol 4-phosphatePhosphatidylinositol PhosphatesPhosphatidylserinesReceptor, IGF Type 2Receptors, SteroidVAPA protein, humanVesicular Transport Proteins

Identifiers

PMID34817532
PMCPMC8624802
OpenAlexW3216159451

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.