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XB-ART-60687
J Biol Chem 2024 May 16;:107373. doi: 10.1016/j.jbc.2024.107373.
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The binding of LARP6 and DNAAF6 in biomolecular condensates influences ciliogenesis of multi-ciliated cells.

Earwood R , Ninomiya H , Wang H , Shimada I , Stroud M , Perez D , Uuganbayar U , Yamada C , Akiyama-Miyoshi T , Stefanovic B , Kato Y .


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Motile cilia on the cell surface produce fluid flows in the body and abnormalities in motile cilia cause primary ciliary dyskinesia (PCD). Dynein axonemal assembly factors 6 (DNAAF6), a causative gene of PCD, was isolated as an interacting protein with La ribonucleoprotein 6 (LARP6) that regulates ciliogenesis in multi-ciliated cells (MCCs). In MCCs of Xenopus embryos, LARP6 and DNAAF6 were co-localized in biomolecular condensates termed dynein axonemal particles (DynAPs) and synergized to control ciliogenesis. Moreover, Tubulin alpha 1c like (TUBA1CL) mRNA encoding α-Tubulin protein that is a major component of ciliary axoneme was identified as a target mRNA regulated by binding LARP6. While DNAAF6 was necessary for high α-Tubulin protein expression near the apical side of Xenopus MCCs during ciliogenesis, its mutant, which abolishes binding with LARP6, was unable to restore the expression of α-Tubulin protein near the apical side of MCCs in Xenopus DNAAF6 morphant. These results indicated that the binding of LARP6 and DNAAF6 in DynAPs regulates highly expressed α-Tubulin protein near the apical side of Xenopus MCCs during ciliogenesis.

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