ArticleBMC biology2022
Bex1 is essential for ciliogenesis and harbours biomolecular condensate-forming capacity.
Article in BMC biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Biological potential and mechanisms of Brain-Expressed X-linked family proteins in cancers: an updated review.Journal of advanced research · 2026Review
- DynAPs and cytoplasmic assembly of axonemal dyneins.Journal of cell science · 2025Article
- KNTC1 introduces segmental heterogeneity to mitochondria.Disease models & mechanisms · 2025Article
- Decoding spatiotemporal transcriptional dynamics and epithelial fibroblast crosstalk during gastroesophageal junction development through single cell analysis.Nature communications · 2024Article
- Novel compound heterozygous variants in theFrontiers in pediatrics · 2024Article
- Identification of Signature Genes of Dilated Cardiomyopathy Using Integrated Bioinformatics Analysis.International journal of molecular sciences · 2023Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPrimary 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.
resultsHere 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.
conclusionsOur data reveals that Bex1 plays an essential role for the primary cilia formation through providing the reaction field for the tubulin polymerization.
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