Evidence map›Paper›PMID 36902293›Full record

ArticleInternational journal of molecular sciences2023

Characterization of a PIP Binding Site in the N-Terminal Domain of V-ATPase a4 and Its Role in Plasma Membrane Association.

Anh Chu, Yeqi Yao, Golam T Saffi, Ji Hyun Chung, Roberto J Botelho, Miroslawa Glibowicka, Charles M Deber, Morris F Manolson

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In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Endosomal Mechanisms in Heart Failure Pathophysiology.Current heart failure reports · 2025
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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

8 authors.

Anh ChuFaculty of Dentistry, University of Toronto, Toronto, ON M5G 1G6, Canada.
Yeqi YaoFaculty of Dentistry, University of Toronto, Toronto, ON M5G 1G6, Canada.
Golam T SaffiDepartment of Pharmacology and Toxicology, University of Toronto, Toronto, ON M5S 1A8, Canada.
Ji Hyun ChungFaculty of Arts and Science, Queen University, Kingston, ON K7L 3N9, Canada.
Roberto J BotelhoDepartment of Chemistry and Biology, Toronto Metropolitan University, Toronto, ON M5G 2A7, Canada.
Miroslawa GlibowickaDivision of Molecular Medicine, Research Institute, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.
Charles M DeberDivision of Molecular Medicine, Research Institute, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.
Morris F ManolsonFaculty of Dentistry, University of Toronto, Toronto, ON M5G 1G6, Canada.ORCID 0000-0001-8755-5460

Funding

CIHR 376666CIHR PJT-148508National Science and Engineering Research Council RGPIN-2022-05169
6 · The paper itself

Abstract

Vacuolar ATPases (V-ATPases) are multi-subunit ATP-dependent proton pumps necessary for cellular functions, including pH regulation and membrane fusion. The evidence suggests that the V-ATPase a-subunit's interaction with the membrane signaling lipid phosphatidylinositol (PIPs) regulates the recruitment of V-ATPase complexes to specific membranes. We generated a homology model of the N-terminal domain of the human a4 isoform (a4NT) using Phyre2.0 and propose a lipid binding domain within the distal lobe of the a4NT. We identified a basic motif, K

Indexed as

Vacuolar Proton-Translocating ATPasesAnimalsBinding SitesCell MembraneHEK293 CellsHumansMammalsPhosphatidylinositolsProtein IsoformsSaccharomyces cerevisiaePhosphatidylinositolsProtein IsoformsVacuolar Proton-Translocating ATPasesdRTAphosphoinositidesPI(4,5)P2protein–lipid interactionV-ATPase a4 isoformsV-ATPases

Identifiers

PMID36902293
PMCPMC10002524

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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.