title: DisAp-dependent striated fiber elongation is required to organize ciliary arrays.
abstract: Cilia-organizing basal bodies (BBs) are microtubule scaffolds that are visibly asymmetrical because they have attached auxiliary structures, such as striated fibers. In multiciliated cells, BB orientation aligns to ensure coherent ciliary beating, but the mechanisms that maintain BB orientation are unclear. For the first time in Tetrahymena thermophila, we use comparative whole-genome sequencing to identify the mutation in the BB disorientation mutant disA-1. disA-1 abolishes the localization of the novel protein DisAp to T. thermophila striated fibers (kinetodesmal fibers; KFs), which is consistent with DisAp's similarity to the striated fiber protein SF-assemblin. We demonstrate that DisAp is required for KFs to elongate and to resist BB disorientation in response to ciliary forces. Newly formed BBs move along KFs as they approach their cortical attachment sites. However, because they contain short KFs that are rotated, BBs in disA-1 cells display aberrant spacing and disorientation. Therefore, DisAp is a novel KF component that is essential for force-dependent KF elongation and BB orientation in multiciliary arrays.
authors.affiliation: Anschutz Medical Campus, Department of Cell and Developmental Biology, University of Colorado, Aurora, CO 80045.
authors.forename: Domenico F
authors.initials: DF
authors.lastname: Galati
authors.affiliation: Anschutz Medical Campus, Department of Cell and Developmental Biology, University of Colorado, Aurora, CO 80045.
authors.forename: Stephanie
authors.initials: S
authors.lastname: Bonney
authors.affiliation: Department of Human Genetics, University of Utah School of Medicine, Salt Lake City, UT 84112.
authors.forename: Zev
authors.initials: Z
authors.lastname: Kronenberg
authors.affiliation: Molecular, Cellular and Developmental Biology, University of Colorado at Boulder, Boulder, CO 80309.
authors.forename: Christina
authors.initials: C
authors.lastname: Clarissa
authors.affiliation: Department of Human Genetics, University of Utah School of Medicine, Salt Lake City, UT 84112.
authors.forename: Mark
authors.initials: M
authors.lastname: Yandell
authors.affiliation: Department of Human Genetics, University of Utah School of Medicine, Salt Lake City, UT 84112.
authors.forename: Nels C
authors.initials: NC
authors.lastname: Elde
authors.affiliation: Department of Cell Biology, M. Nencki Institute of Experimental Biology, 02-093 Warsaw, Poland.
authors.forename: Maria
authors.initials: M
authors.lastname: Jerka-Dziadosz
authors.affiliation: Molecular, Cellular and Developmental Biology, University of Colorado at Boulder, Boulder, CO 80309.
authors.forename: Thomas H
authors.initials: TH
authors.lastname: Giddings
authors.affiliation: Department of Biological Sciences, University of Iowa, Iowa City, IA 52242.
authors.forename: Joseph
authors.initials: J
authors.lastname: Frankel
authors.affiliation: Anschutz Medical Campus, Department of Cell and Developmental Biology, University of Colorado, Aurora, CO 80045 Chad.Pearson@ucdenver.edu.
authors.forename: Chad G
authors.initials: CG
authors.lastname: Pearson
mesh_terms: D001696:Biomechanical Phenomena; D002923:Cilia / Q000378:metabolism* / Q000648:ultrastructure; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism / Q000648:ultrastructure; D010802:Phylogeny; D015800:Protozoan Proteins / Q000235:genetics / Q000378:metabolism*; D016808:Tetrahymena thermophila / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure*
chemical_list: D008869:Microtubule-Associated Proteins; D015800:Protozoan Proteins; C096668:striated fiber assemblin