Lysine Demethylase 4A (KDM4A) Maintains Basal Body Architecture and Protects Against Ciliary Destabilization
Motrapu, M.; Hudson, L.; Chowdhury, P.; Wang, X.; Nakatani, Y.; Vargas-Hernandez, S.; Jung, S. Y.; Karki, M.; Walker, C. L.; Gustavsson, A.-K.; Dere, R.
Show 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 KDM4A 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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