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DisAp-dependent striated fiber elongation is required to organize ciliary arrays
Authors:Domenico F. Galati  Stephanie Bonney  Zev Kronenberg  Christina Clarissa  Mark Yandell  Nels C. Elde  Maria Jerka-Dziadosz  Thomas H. Giddings  Joseph Frankel  Chad G. Pearson
Affiliation:1.Anschutz Medical Campus, Department of Cell and Developmental Biology, University of Colorado, Aurora, CO 80045;2.Department of Human Genetics, University of Utah School of Medicine, Salt Lake City, UT 84112;3.Molecular, Cellular and Developmental Biology, University of Colorado at Boulder, Boulder, CO 80309;4.Department of Cell Biology, M. Nencki Institute of Experimental Biology, 02-093 Warsaw, Poland;5.Department of Biological Sciences, University of Iowa, Iowa City, IA 52242
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.
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