Evidence map›Paper›PMID 24554764›Full record

ArticleMolecular biology of the cell2014

Kdm3a lysine demethylase is an Hsp90 client required for cytoskeletal rearrangements during spermatogenesis.

Ioannis Kasioulis, Heather M Syred, Peri Tate, Andrew Finch, Joseph Shaw, Anne Seawright, Matt Fuszard, Catherine H Botting, Sally Shirran, Ian R Adams and 3 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Human sperm RNA in male infertility.Nature reviews. Urology · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Epigenetics: A key paradigm in reproductive health.Clinical and experimental reproductive medicine · 2016
    Review
  19. Review
  20. 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

13 authors at 3 institutions in 1 country.

Ioannis KasioulisMRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, Western General Hospital, University of Edinburgh, Edinburgh EH4 2XU, United Kingdom Edinburgh Cancer Research UK Centre, Institute of Genetics and Molecular Medicine, Western General Hospital, University of Edinburgh, Edinburgh EH4 2XU, United Kingdom Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Cambridge CB10 1HH, United Kingdom Biomedical Sciences Research Complex Mass Spectrometry and Proteomics Facility, University of St. Andrews, St. Andrews, Fife KY16 9ST, United Kingdom.
Heather M Syred
Peri Tate
Andrew Finch
Joseph Shaw
Anne Seawright
Matt Fuszard
Catherine H Botting
Sally Shirran
Ian R Adams
Ian J Jackson
Veronica van Heyningen
Patricia L Yeyati
Western General Hospital · GBUniversity of St Andrews · GBWellcome Sanger Institute · GB

Funding

Medical Research Council MC_PC_U127527199Medical Research Council MC_PC_U127561112Medical Research Council MC_U127527199Wellcome Trust
6 · The paper itself

Abstract

The lysine demethylase Kdm3a (Jhdm2a, Jmjd1a) is required for male fertility, sex determination, and metabolic homeostasis through its nuclear role in chromatin remodeling. Many histone-modifying enzymes have additional nonhistone substrates, as well as nonenzymatic functions, contributing to the full spectrum of events underlying their biological roles. We present two Kdm3a mouse models that exhibit cytoplasmic defects that may account in part for the globozoospermia phenotype reported previously. Electron microscopy revealed abnormal acrosome and manchette and the absence of implantation fossa at the caudal end of the nucleus in mice without Kdm3a demethylase activity, which affected cytoplasmic structures required to elongate the sperm head. We describe an enzymatically active new Kdm3a isoform and show that subcellular distribution, protein levels, and lysine demethylation activity of Kdm3a depended on Hsp90. We show that Kdm3a localizes to cytoplasmic structures of maturing spermatids affected in Kdm3a mutant mice, which in turn display altered fractionation of β-actin and γ-tubulin. Kdm3a is therefore a multifunctional Hsp90 client protein that participates directly in the regulation of cytoskeletal components.

Indexed as

AcrosomeActinsAnimalsAzoospermiaCell LineCloning, MolecularCytoskeletonHSP90 Heat-Shock ProteinsHumansJumonji Domain-Containing Histone DemethylasesMaleMiceMice, Inbred C57BLMice, TransgenicProtein IsoformsRetinal Pigment EpitheliumActinsHSP90 Heat-Shock ProteinsJumonji Domain-Containing Histone DemethylasesKdm3a protein, mouseProtein IsoformsTubulin

Identifiers

PMID24554764
PMCPMC3982988
OpenAlexW2104520045

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.