Evidence map›Paper›PMID 29916806›Full record

ArticleeLife2018

ZMYND10 functions in a chaperone relay during axonemal dynein assembly.

Girish R Mali, Patricia L Yeyati, Seiya Mizuno, Daniel O Dodd, Peter A Tennant, Margaret A Keighren, Petra Zur Lage, Amelia Shoemark, Amaya Garcia-Munoz, Atsuko Shimada and 6 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

40 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. A homozygous splice-site variant inFrontiers in medicine · 2026
    Article
  3. Article
  4. Molecular basis for the activation of outer dynein arms in cilia.Nature structural & molecular biology · 2025
    Article
  5. Article
  6. Review
  7. Identification of novel interacting proteins of FUZ and GPR161.bioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Case Report: Minigene assays reveal a novelFrontiers in genetics · 2025
    Article
  12. Cotranslational molecular condensation of cochaperones and assembly factors facilitates axonemal dynein biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Review
  14. Article
  15. Formation and function of multiciliated cells.The Journal of cell biology · 2024
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

16 authors at 8 institutions in 4 countries.

Girish R Mali *MRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom.ORCID http://orcid.org/0000-0002-5551-7555
Patricia L Yeyati *MRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom.ORCID http://orcid.org/0000-0001-5094-5182
Seiya MizunoLaboratory Animal Resource Centre, University of Tsukuba, Tsukuba, Japan.
Daniel O DoddMRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom.
Peter A TennantMRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom.
Margaret A KeighrenMRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom.
Petra Zur LageCentre for Discovery Brain Sciences, University of Edinburgh, Edinburgh, United Kingdom.
Amelia ShoemarkDivision of Molecular and Clinical Medicine, University of Dundee, Dundee, United Kingdom.
Amaya Garcia-MunozSystems Biology Ireland, University College Dublin, Dublin, Ireland.
Atsuko ShimadaDepartment of Biological Sciences, University of Tokyo, Tokyo, Japan.
Hiroyuki TakedaDepartment of Biological Sciences, University of Tokyo, Tokyo, Japan.
Frank EdlichInstitute for Biochemistry and Molecular Biology, University of Freiburg, Freiburg, Germany.
Satoru TakahashiLaboratory Animal Resource Centre, University of Tsukuba, Tsukuba, Japan.
Alex von KreigsheimSystems Biology Ireland, University College Dublin, Dublin, Ireland.
Andrew P JarmanCentre for Discovery Brain Sciences, University of Edinburgh, Edinburgh, United Kingdom.ORCID https://orcid.org/0000-0003-4036-5701
Pleasantine MillMRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom.ORCID http://orcid.org/0000-0001-5218-134X
Institute of Genetics and Cancer · GBThe University of Tokyo · JPUniversity College Dublin · IEUniversity of Edinburgh · GBUniversity of Tsukuba · JPMRC Laboratory of Molecular Biology · GBUniversity of Dundee · GBUniversity of Freiburg · DE

Funding

Medical Research Council MC_UU_00007/14Medical Research Council MC_UU_12018/26Medical Research Council MRC_UU_12018/26
6 · The paper itself

Abstract

Molecular chaperones promote the folding and macromolecular assembly of a diverse set of 'client' proteins. How ubiquitous chaperone machineries direct their activities towards specific sets of substrates is unclear. Through the use of mouse genetics, imaging and quantitative proteomics we uncover that ZMYND10 is a novel co-chaperone that confers specificity for the FKBP8-HSP90 chaperone complex towards axonemal dynein clients required for cilia motility. Loss of ZMYND10 perturbs the chaperoning of axonemal dynein heavy chains, triggering broader degradation of dynein motor subunits. We show that pharmacological inhibition of FKBP8 phenocopies dynein motor instability associated with the loss of ZMYND10 in airway cells and that human disease-causing variants of ZMYND10 disrupt its ability to act as an FKBP8-HSP90 co-chaperone. Our study indicates that primary ciliary dyskinesia (PCD), caused by mutations in dynein assembly factors disrupting cytoplasmic pre-assembly of axonemal dynein motors, should be considered a cell-type specific protein-misfolding disease.

Indexed as

AnimalsAnimals, NewbornAxonemeBase SequenceBrainCell LineCiliaCytoskeletal ProteinsDNA-Binding ProteinsDyneinsEpithelial CellsGene Expression RegulationHEK293 CellsHSP90 Heat-Shock ProteinsHumansMiceCytoskeletal ProteinsDNA-Binding ProteinsDyneinsFkbp8 protein, mouseHSP90 Heat-Shock ProteinsMolecular ChaperonesTacrolimus Binding ProteinsZMYND10 protein, mousecell biologychaperoneciliadevelopmental biologyD. melanogasterdyneinhumanhuman diseasemacromolecular assemblymouseproteastasisregenerative medicinestem cells

Identifiers

PMID29916806
PMCPMC6044906
OpenAlexW2782243842

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.