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Tubulin glycylases and glutamylases have distinct functions in stabilization and motility of ependymal cilia
Authors:Montserrat Bosch Grau  Gloria Gonzalez Curto  Cecilia Rocha  Maria M Magiera  Patricia Marques Sousa  Tiziana Giordano  Nathalie Spassky  Carsten Janke
Institution:1.Institut Curie, 91405 Orsay, France;2.Centre National de la Recherche Scientifique (CNRS) UMR3306, 91405 Orsay, France;3.Institut National de la Santé et de la Recherche Médicale (INSERM) U1005, 91405 Orsay, France;4.PSL Research University, 75005 Paris, France;5.Ecole Normale Supérieure (ENS), Institut de Biologie de l’ENS, 75005 Paris, France;6.INSERM U1024, 75005 Paris, France;7.CNRS UMR8197, 75005 Paris, France
Abstract:Microtubules are subject to a variety of posttranslational modifications that potentially regulate cytoskeletal functions. Two modifications, glutamylation and glycylation, are highly enriched in the axonemes of most eukaryotes, and might therefore play particularly important roles in cilia and flagella. Here we systematically analyze the dynamics of glutamylation and glycylation in developing mouse ependymal cilia and the expression of the corresponding enzymes in the brain. By systematically screening enzymes of the TTLL family for specific functions in ependymal cilia, we demonstrate that the glycylating enzymes TTLL3 and TTLL8 were required for stability and maintenance of ependymal cilia, whereas the polyglutamylase TTLL6 was necessary for coordinated beating behavior. Our work provides evidence for a functional separation of glutamylating and glycylating enzymes in mammalian ependymal cilia. It further advances the elucidation of the functions of tubulin posttranslational modifications in motile cilia of the mammalian brain and their potential importance in brain development and disease.
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