Evidence map›Paper›PMID 35994636›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Identification of mEAK-7 as a human V-ATPase regulator via cryo-EM data mining.

Longfei Wang, Di Wu, Carol V Robinson, Tian-Min Fu

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

12 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. ATG16L1 controls mammalian vacuolar proton ATPase.The Journal of cell biology · 2025
    Article
  3. Article
  4. Article
  5. Oxr1 and Ncoa7 regulate V-ATPase to achieve optimal pH for glycosylation within the Golgi apparatus and trans-Golgi network.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Interaction of yeast V-ATPase with TLDc protein Rtc5p.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Article
  9. Defective Lamtor5 Leads to Autoimmunity by Deregulating v-ATPase and Lysosomal Acidification.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  10. Article
  11. Review
  12. Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.BioEssays : news and reviews in molecular, cellular and developmental biology · 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

4 authors at 3 institutions in 3 countries.

Longfei WangDepartment of Cardiology, Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan 430071, China.
Di WuDepartment of Chemistry, University of Oxford, Oxford OX1 3QZ, United Kingdom.
Carol V RobinsonDepartment of Chemistry, University of Oxford, Oxford OX1 3QZ, United Kingdom.ORCID 0000-0001-7829-5505
Tian-Min FuDepartment of Biological Chemistry and Pharmacology, The Ohio State University, Columbus, OH 43210.ORCID 0000-0002-6281-1752
University of Oxford · GBThe Ohio State University · USWuhan University · CN

Funding

TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
MOLECULAR MECHANISMS OF V-ATPASES: ASSEMBLY, BIOGENESIS, REGULATION, AND FUNCTIONR35GM147465 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI Tianmin Fu · 2022 to 2026
$2.1M
NIGMS NIH HHS P41 GM103310NIGMS NIH HHS R35 GM147465
6 · The paper itself

Abstract

Vacuolar-type adenosine triphosphatases (V-ATPases) not only function as rotary proton pumps in cellular organelles but also serve as signaling hubs. To identify the endogenous binding partners of V-ATPase, we collected a large dataset of human V-ATPases and did extensive classification and focused refinement of human V-ATPases. Unexpectedly, about 17% of particles in state 2 of human V-ATPases display additional density with an overall resolution of 3.3 Å. Structural analysis combined with artificial intelligence modeling enables us to identify this additional density as mEAK-7, a protein involved in mechanistic target of rapamycin (mTOR) signaling in mammals. Our structure shows that mEAK-7 interacts with subunits A, B, D, and E of V-ATPases in state 2. Thus, we propose that mEAK-7 may regulate V-ATPase function through binding to V-ATPases in state 2 as well as mediate mTOR signaling.

Indexed as

Cryoelectron MicroscopyData MiningVacuolar Proton-Translocating ATPasesAnimalsArtificial IntelligenceHumansMammalsProtein BindingTOR Serine-Threonine KinasesTOR Serine-Threonine KinasesVacuolar Proton-Translocating ATPaseslysosomal signalingmEAK-7mTORV-ATPase

Identifiers

PMID35994636
PMCPMC9436323
OpenAlexW4292651814

What OpenQuestion holds

Textmetadata
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.