@article{oai:shiga-med.repo.nii.ac.jp:00004128,
 author = {日比野, 絵美 and 一山, 悠介 and 塚村, 篤史 and 森宗, 孝夫 and 大路, 正人 and 丸尾, 良浩 and 西村, 正樹 and 森, 雅樹 and HIBINO, Emi and ICHIYAMA, Yusuke and TSUKAMURA, Atsushi and SENJU, Yosuke and MORIMUNE, Takao and OHJI, Masahito and MARUO, Yoshihiro and NISHIMURA, Masaki and MORI, Masaki},
 issue = {1},
 journal = {BMC Biology},
 month = {Feb},
 note = {pdf, Background:
Primary cilia are sensory organelles crucial for organ development. The pivotal structure of the primary cilia is a microtubule that is generated via tubulin polymerization reaction that occurs in the basal body. It remains to be elucidated how molecules with distinct physicochemical properties contribute to the formation of the primary cilia., Results:
Here we show that brain expressed X-linked 1 (Bex1) plays an essential role in tubulin polymerization and primary cilia formation. The Bex1 protein shows the physicochemical property of being an intrinsically disordered protein (IDP). Bex1 shows cell density-dependent accumulation as a condensate either in nucleoli at a low cell density or at the apical cell surface at a high cell density. The apical Bex1 localizes to the basal body. Bex1 knockout mice present ciliopathy phenotypes and exhibit ciliary defects in the retina and striatum. Bex1 recombinant protein shows binding capacity to guanosine triphosphate (GTP) and forms the condensate that facilitates tubulin polymerization in the reconstituted system., Conclusions:
Our data reveals that Bex1 plays an essential role for the primary cilia formation through providing the reaction field for the tubulin polymerization., Journal Article},
 title = {Bex1 is essential for ciliogenesis and harbours biomolecular condensate-forming capacity.},
 volume = {20},
 year = {2022}
}