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      Ciliary proteins Fap43 and Fap44 interact with each other and are essential for proper cilia and flagella beating

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          Abstract

          Cilia beating is powered by the inner and outer dynein arms (IDAs and ODAs). These multi-subunit macrocomplexes are arranged in two rows on each outer doublet along the entire cilium length, except its distal end. To generate cilia beating, the activity of ODAs and IDAs must be strictly regulated locally by interactions with the dynein arm-associated structures within each ciliary unit and coordinated globally in time and space between doublets and along the axoneme. Here, we provide evidence of a novel ciliary complex composed of two conserved WD-repeat proteins, Fap43p and Fap44p. This complex is adjacent to another WD-repeat protein, Fap57p, and most likely the two-headed inner dynein arm, IDA I1. Loss of either protein results in altered waveform, beat stroke and reduced swimming speed. The ciliary localization of Fap43p and Fap44p is interdependent in the ciliate Tetrahymena thermophila.

          Electronic supplementary material

          The online version of this article (10.1007/s00018-018-2819-7) contains supplementary material, which is available to authorized users.

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          Most cited references 50

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          SEAVIEW and PHYLO_WIN: two graphic tools for sequence alignment and molecular phylogeny.

          SEAVIEW and PHYLO_WIN are two graphic tools for X Windows-Unix computers dedicated to sequence alignment and molecular phylogenetics. SEAVIEW is a sequence alignment editor allowing manual or automatic alignment through an interface with CLUSTALW program. Alignment of large sequences with extensive length differences is made easier by a dot-plot-based routine. The PHYLO_WIN program allows phylogenetic tree building according to most usual methods (neighbor joining with numerous distance estimates, maximum parsimony, maximum likelihood), and a bootstrap analysis with any of them. Reconstructed trees can be drawn, edited, printed, stored, evaluated according to numerous criteria. Taxonomic species groups and sets of conserved regions can be defined by mouse and stored into sequence files, thus avoiding multiple data files. Both tools are entirely mouse driven. On-line help makes them easy to use. They are freely available by anonymous ftp at biom3.univ-lyon1.fr/pub/ mol_phylogeny or http:@acnuc.univ-lyon1.fr/, or by e-mail to galtier@biomserv.univ-lyon1.fr.
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            Comparative genomics identifies a flagellar and basal body proteome that includes the BBS5 human disease gene.

            Cilia and flagella are microtubule-based structures nucleated by modified centrioles termed basal bodies. These biochemically complex organelles have more than 250 and 150 polypeptides, respectively. To identify the proteins involved in ciliary and basal body biogenesis and function, we undertook a comparative genomics approach that subtracted the nonflagellated proteome of Arabidopsis from the shared proteome of the ciliated/flagellated organisms Chlamydomonas and human. We identified 688 genes that are present exclusively in organisms with flagella and basal bodies and validated these data through a series of in silico, in vitro, and in vivo studies. We then applied this resource to the study of human ciliation disorders and have identified BBS5, a novel gene for Bardet-Biedl syndrome. We show that this novel protein localizes to basal bodies in mouse and C. elegans, is under the regulatory control of daf-19, and is necessary for the generation of both cilia and flagella.
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              A Size-Exclusion Permeability Barrier and Nucleoporins Characterize a Ciliary Pore Complex that Regulates Transport into Cilia

              The cilium is a microtubule-based organelle that contains a unique complement of proteins for cell motility and signaling functions. Entry into the ciliary compartment is proposed to be regulated at the base of the cilium 1 . Recent work demonstrated that components of the nuclear import machinery, including the RanGTPase and importins, regulate ciliary entry 2–4 . We hypothesized that the ciliary base contains a ciliary pore complex (CPC) whose molecular nature and selective mechanism are similar to the nuclear pore complex (NPC). By microinjecting fluorescently-labeled dextrans and recombinant proteins of various sizes, we characterize a size-dependent diffusion barrier for the entry of cytoplasmic molecules into primary cilia in mammalian cells. We demonstrate that nucleoporins localize to the base of primary and motile cilia and that microinjection of nucleoporin function-blocking reagents blocks the ciliary entry of kinesin-2 KIF17 motors. Together, this work demonstrates that the physical and molecular nature of the CPC is similar to the NPC, and further extends functional parallels between nuclear and ciliary import.
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                Author and article information

                Contributors
                +4822 58 92 338 , p.urbanska@nencki.gov.pl
                +4822 58 92 281 , e.joachimiak@nencki.gov.pl
                +4822 58 92 338 , r.bazan@nencki.gov.pl
                +1 214-645-1561 , Gang.Fu@UTSouthwestern.edu
                +4822 58 92 338 , m.poprzeczko@nencki.gov.pl
                +4822 58 92 338 , h.fabczak@nencki.gov.pl
                +1 214-648-3925 , Daniela.Nicastro@UTSouthwestern.edu
                +4822 58 92 338 , d.wloga@nencki.gov.pl
                Journal
                Cell Mol Life Sci
                Cell. Mol. Life Sci
                Cellular and Molecular Life Sciences
                Springer International Publishing (Cham )
                1420-682X
                1420-9071
                23 April 2018
                23 April 2018
                2018
                : 75
                : 24
                : 4479-4493
                Affiliations
                [1 ]ISNI 0000 0001 1943 2944, GRID grid.419305.a, Laboratory of Cytoskeleton and Cilia Biology, Department of Cell Biology, , Nencki Institute of Experimental Biology PAS, ; Pasteur 3, 02-093 Warsaw, Poland
                [2 ]ISNI 0000 0000 9482 7121, GRID grid.267313.2, Departments of Cell Biology and Biophysics, , University of Texas Southwestern Medical Center, ; 6000 Harry Hines Blvd., Dallas, TX USA
                Article
                2819
                10.1007/s00018-018-2819-7
                6208767
                29687140
                © The Author(s) 2018

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

                Funding
                Funded by: Polskie Ministerstwo Nauki i Szkolnictwa Wyższego
                Award ID: N301706640
                Award Recipient :
                Funded by: Narodowe Centrum Nauki, Polska
                Award ID: 2014/14/M/NZ3/00511
                Award Recipient :
                Funded by: FundRef http://dx.doi.org/10.13039/100004410, European Molecular Biology Organization;
                Award ID: Installation Grant no. 2331
                Award Recipient :
                Funded by: Narodowe Centrum Nauki (PL)
                Award ID: 2014/13/N/NZ3/04612
                Award Recipient :
                Funded by: FundRef http://dx.doi.org/10.13039/100000002, National Institutes of Health;
                Award ID: R01 GM083122
                Award Recipient :
                Categories
                Original Article
                Custom metadata
                © Springer Nature Switzerland AG 2018

                Molecular biology

                wdr65, wdr52, wdr96, dyh6, dyh7, tether/tether head complex

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