Evidence map›Paper›PMID 33340069›Full record

ArticleCellular and molecular life sciences : CMLS2021

The Ncoa7 locus regulates V-ATPase formation and function, neurodevelopment and behaviour.

Enrico Castroflorio, Joery den Hoed, Daria Svistunova, Mattéa J Finelli, Alberto Cebrian-Serrano, Silvia Corrochano, Andrew R Bassett, Benjamin Davies, Peter L Oliver

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

35 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
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  9. 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
  10. Interaction of yeast V-ATPase with TLDc protein Rtc5p.bioRxiv : the preprint server for biology · 2025
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  13. Review
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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

9 authors at 5 institutions in 2 countries.

Enrico CastroflorioMRC Harwell Institute, Harwell Campus, Oxfordshire, OX11 0RD, UK.
Joery den HoedDepartment of Physiology, Anatomy and Genetics, University of Oxford, Parks Road, Oxford, OX1 3PT, UK.
Daria SvistunovaDepartment of Physiology, Anatomy and Genetics, University of Oxford, Parks Road, Oxford, OX1 3PT, UK.
Mattéa J FinelliDepartment of Physiology, Anatomy and Genetics, University of Oxford, Parks Road, Oxford, OX1 3PT, UK.
Alberto Cebrian-SerranoWellcome Centre for Human Genetics, Roosevelt Drive, Oxford, OX3 7BN, UK.
Silvia CorrochanoMRC Harwell Institute, Harwell Campus, Oxfordshire, OX11 0RD, UK.
Andrew R BassettWellcome Sanger Institute, Wellcome Genome Campus, Hinxton, Cambridge, CB10 1SA, UK.
Benjamin DaviesWellcome Centre for Human Genetics, Roosevelt Drive, Oxford, OX3 7BN, UK.
Peter L OliverMRC Harwell Institute, Harwell Campus, Oxfordshire, OX11 0RD, UK. p.oliver@har.mrc.ac.uk.ORCID http://orcid.org/0000-0003-3347-2461
University of Oxford · GBCentre for Human Genetics · GBHospital Clínico San Carlos · ESMary Lyon Centre at MRC Harwell · GBWellcome Sanger Institute · GB

Funding

Medical Research Council MC_EX_MR/P502005/1Wellcome TrustWellcome Trust 203141/Z/16/Z
6 · The paper itself

Abstract

Members of the Tre2/Bub2/Cdc16 (TBC), lysin motif (LysM), domain catalytic (TLDc) protein family are associated with multiple neurodevelopmental disorders, although their exact roles in disease remain unclear. For example, nuclear receptor coactivator 7 (NCOA7) has been associated with autism, although almost nothing is known regarding the mode-of-action of this TLDc protein in the nervous system. Here we investigated the molecular function of NCOA7 in neurons and generated a novel mouse model to determine the consequences of deleting this locus in vivo. We show that NCOA7 interacts with the cytoplasmic domain of the vacuolar (V)-ATPase in the brain and demonstrate that this protein is required for normal assembly and activity of this critical proton pump. Neurons lacking Ncoa7 exhibit altered development alongside defective lysosomal formation and function; accordingly, Ncoa7 deletion animals exhibited abnormal neuronal patterning defects and a reduced expression of lysosomal markers. Furthermore, behavioural assessment revealed anxiety and social defects in mice lacking Ncoa7. In summary, we demonstrate that NCOA7 is an important V-ATPase regulatory protein in the brain, modulating lysosomal function, neuronal connectivity and behaviour; thus our study reveals a molecular mechanism controlling endolysosomal homeostasis that is essential for neurodevelopment.

Indexed as

Behavior, AnimalDisease Models, AnimalOxidative StressAnimalsEndosomesFemaleLysosomesMiceMice, Inbred C57BLMice, KnockoutNeurodevelopmental DisordersNeuronsNuclear Receptor CoactivatorsVacuolar Proton-Translocating ATPasesNcoa7 protein, mouseNuclear Receptor CoactivatorsVacuolar Proton-Translocating ATPasesAutismBehaviourLysosomeMouseNeurodevelopmentNeuronV-ATPase

Identifiers

PMID33340069
PMCPMC8038996
OpenAlexW3114060472

What OpenQuestion holds

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LicenceCC BY
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.