Lysine Demethylase 4A (KDM4A) Maintains Basal Body Architecture and Protects Against Ciliary Destabilization

Primary cilia are sensory organelles essential for signaling and defects in formation, maintenance or structure underlie diverse ciliopathies. Here, we identify lysine demethylase 4A (KDM4A) as a previously unrecognized mediator of ciliogenesis. Using genetic depletion and pharmacologic inhibition, we show that KDM4A is required for cilia assembly and maintenance. Super-resolution imaging reveals KDM4A localization at the basal body, where it distinctively wraps around the centrioles. We uncover a direct interaction between KDM4A and Rootletin (CROCC), a structural protein mediating centriole cohesion, and demonstrate that <i>KDM4A</i> loss increases inter-centriolar distances, implicating basal body architecture in ciliary failure. Together, these findings define a demethylase-centrosome axis that integrates KDM4A activity with organelle biology, revealing new mechanisms underlying ciliogenesis.

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Publication Details

Journal
bioRxiv (Cold Spring Harbor Laboratory)
Published
2026-02-02
DOI
https://doi.org/10.64898/2026.01.30.702865
Primary Topic
Genetic and Kidney Cyst Diseases
Type
article
Field-Weighted Citation Impact
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article

Lysine Demethylase 4A (KDM4A) Maintains Basal Body Architecture and Protects Against Ciliary Destabilization

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bioRxiv (Cold Spring Harbor Laboratory)
Genetic and Kidney Cyst Diseases
article

Lysine Demethylase 4A (KDM4A) Maintains Basal Body Architecture and Protects Against Ciliary Destabilization

Anna‐Karin Gustavsson, Sofía Vargas-Hernández, Yuya Nakatani, X Wang, Pratim Chowdhury, Manga Motrapu, Sung Yun Jung, Lindsey Hudson, Cheryl L Walker, Ruhee Dere, Menuka Karki
article en

Abstract

Primary cilia are sensory organelles essential for signaling and defects in formation, maintenance or structure underlie diverse ciliopathies. Here, we identify lysine demethylase 4A (KDM4A) as a previously unrecognized mediator of ciliogenesis. Using genetic depletion and pharmacologic inhibition, we show that KDM4A is required for cilia assembly and maintenance. Super-resolution imaging reveals KDM4A localization at the basal body, where it distinctively wraps around the centrioles. We uncover a direct interaction between KDM4A and Rootletin (CROCC), a structural protein mediating centriole cohesion, and demonstrate that <i>KDM4A</i> loss increases inter-centriolar distances, implicating basal body architecture in ciliary failure. Together, these findings define a demethylase-centrosome axis that integrates KDM4A activity with organelle biology, revealing new mechanisms underlying ciliogenesis.

bioRxiv (Cold Spring Harbor Laboratory)
The University of Texas MD Anderson Cancer Center (US), Baylor College of Medicine (US), Rice University (US)
U.S. Department of Defense, Cancer Prevention and Research Institute of Texas, Rice University, National Institutes of Health, National Cancer Institute, National Institute of General Medical Sciences, National Institute of Environmental Health Sciences, Congressionally Directed Medical Research Programs
Openalex Percentile: Top 66%
Genetic and Kidney Cyst Diseases
DOIOpen Access PDFOpenAlex
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