title: A migrating ciliary gate compartmentalizes the site of axoneme assembly in Drosophila spermatids.
abstract: BACKGROUND
  In most cells, the cilium is formed within a compartment separated from the cytoplasm. Entry into the ciliary compartment is regulated by a specialized gate located at the base of the cilium in a region known as the transition zone. The transition zone is closely associated with multiple structures of the ciliary base, including the centriole, axoneme, and ciliary membrane. However, the contribution of these structures to the ciliary gate remains unclear.
  
  
  RESULTS
  Here we report that, in Drosophila spermatids, a conserved module of transition zone proteins mutated in Meckel-Gruber syndrome (MKS), including Cep290, Mks1, B9d1, and B9d2, comprise a ciliary gate that continuously migrates away from the centriole to compartmentalize the growing axoneme tip. We show that Cep290 is essential for transition zone composition, compartmentalization of the axoneme tip, and axoneme integrity and find that MKS proteins also delimit a centriole-independent compartment in mouse spermatids.
  
  
  CONCLUSIONS
  Our findings demonstrate that the ciliary gate can migrate away from the base of the cilium, thereby functioning independently of the centriole and of a static interaction with the axoneme to compartmentalize the site of axoneme assembly.
authors.affiliation: Department of Biological Sciences, University of Toledo, 3050 W. Towerview Boulevard, Toledo, OH 43606, USA.
authors.forename: Marcus L
authors.initials: ML
authors.lastname: Basiri
authors.affiliation: Department of Biological Sciences, University of Toledo, 3050 W. Towerview Boulevard, Toledo, OH 43606, USA.
authors.forename: Andrew
authors.initials: A
authors.lastname: Ha
authors.affiliation: Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA.
authors.forename: Abhishek
authors.initials: A
authors.lastname: Chadha
authors.affiliation: Department of Biological Sciences, University of Toledo, 3050 W. Towerview Boulevard, Toledo, OH 43606, USA.
authors.forename: Nicole M
authors.initials: NM
authors.lastname: Clark
authors.affiliation: Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, Prospekt Toreza, 44, 194223 St. Petersburg, Russia.
authors.forename: Andrey
authors.initials: A
authors.lastname: Polyanovsky
authors.affiliation: Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA.
authors.forename: Boaz
authors.initials: B
authors.lastname: Cook
authors.affiliation: Department of Biological Sciences, University of Toledo, 3050 W. Towerview Boulevard, Toledo, OH 43606, USA. Electronic address: tomer.avidorreiss@utoledo.edu.
authors.forename: Tomer
authors.initials: T
authors.lastname: Avidor-Reiss
mesh_terms: D000818:Animals; D054468:Axoneme / Q000378:metabolism* / Q000648:ultrastructure; D002923:Cilia / Q000378:metabolism / Q000648:ultrastructure; D004330:Drosophila / Q000166:cytology* / Q000378:metabolism; D029721:Drosophila Proteins / Q000032:analysis / Q000378:metabolism / Q000502:physiology; D008297:Male; D051379:Mice; D008869:Microtubule-Associated Proteins / Q000032:analysis / Q000378:metabolism / Q000502:physiology; D013087:Spermatids / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: D029721:Drosophila Proteins; D008869:Microtubule-Associated Proteins; C000600530:centrosomal protein 290, Drosophila