title: The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate.
abstract: Transition fibres (TFs), together with the transition zone (TZ), are basal ciliary structures thought to be crucial for cilium biogenesis and function by acting as a ciliary gate to regulate selective protein entry and exit. Here we demonstrate that the centriolar and basal body protein HYLS-1, the C. elegans orthologue of hydrolethalus syndrome protein 1, is required for TF formation, TZ organization and ciliary gating. Loss of HYLS-1 compromises the docking and entry of intraflagellar transport (IFT) particles, ciliary gating for both membrane and soluble proteins, and axoneme assembly. Additional depletion of the TF component DYF-19 in hyls-1 mutants further exacerbates TZ anomalies and completely abrogates ciliogenesis. Our data support an important role for HYLS-1 and TFs in establishment of the ciliary gate and underline the importance of selective protein entry for cilia assembly.
authors.affiliation: Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.|Key Laboratory of Insect Developmental and Evolutionary Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China.
authors.forename: Qing
authors.initials: Q
authors.lastname: Wei
authors.affiliation: Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
authors.forename: Yingyi
authors.initials: Y
authors.lastname: Zhang
authors.affiliation: Max F. Perutz Laboratories, Vienna Biocenter (VBC), University of Vienna, A-1030 Vienna, Austria.
authors.forename: Clementine
authors.initials: C
authors.lastname: Schouteden
authors.affiliation: Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
authors.forename: Yuxia
authors.initials: Y
authors.lastname: Zhang
authors.affiliation: Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
authors.forename: Qing
authors.initials: Q
authors.lastname: Zhang
authors.affiliation: Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
authors.forename: Jinhong
authors.initials: J
authors.lastname: Dong
authors.affiliation: Max F. Perutz Laboratories, Vienna Biocenter (VBC), University of Vienna, A-1030 Vienna, Austria.
authors.forename: Veronika
authors.initials: V
authors.lastname: Wonesch
authors.affiliation: Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
authors.forename: Kun
authors.initials: K
authors.lastname: Ling
authors.affiliation: Max F. Perutz Laboratories, Vienna Biocenter (VBC), University of Vienna, A-1030 Vienna, Austria.
authors.forename: Alexander
authors.initials: A
authors.lastname: Dammermann
authors.affiliation: Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.|Division of Nephrology and Hypertension, Mayo Clinic, Rochester, Minnesota 55905, USA.|Mayo Translational PKD Center, Mayo Clinic, Rochester, Minnesota 55905, USA.
authors.forename: Jinghua
authors.initials: J
authors.lastname: Hu
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans; D029742:Caenorhabditis elegans Proteins / Q000378:metabolism*; D002923:Cilia / Q000378:metabolism* / Q000648:ultrastructure; D005407:Flagella / Q000378:metabolism; D017353:Gene Deletion; D006228:Hand Deformities, Congenital / Q000378:metabolism*; D006330:Heart Defects, Congenital / Q000378:metabolism*; D006849:Hydrocephalus / Q000378:metabolism*; D008954:Models, Biological; D038081:Organogenesis
chemical_list: D029742:Caenorhabditis elegans Proteins; C543513:HYLS-1 protein, C elegans