a wntbeta-catenin pathway antagonist chibby binds cenexin at the distal end of mother centrioles and functions in primary cilia formationwntbeta-catenin通道拮抗剂chibby结合cenexin母亲的远端中心粒和功能在初级纤毛的形成.pdfVIP

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a wntbeta-catenin pathway antagonist chibby binds cenexin at the distal end of mother centrioles and functions in primary cilia formationwntbeta-catenin通道拮抗剂chibby结合cenexin母亲的远端中心粒和功能在初级纤毛的形成.pdf

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a wntbeta-catenin pathway antagonist chibby binds cenexin at the distal end of mother centrioles and functions in primary cilia formationwntbeta-catenin通道拮抗剂chibby结合cenexin母亲的远端中心粒和功能在初级纤毛的形成

A Wnt/beta-Catenin Pathway Antagonist Chibby Binds Cenexin at the Distal End of Mother Centrioles and Functions in Primary Cilia Formation 1 1 2,3 4 2,3,4 Nathan Steere , Vanessa Chae , Michael Burke , Feng-Qian Li , Ken-Ichi Takemaru , Ryoko Kuriyama1* 1 Department of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, Minnesota, United States of America, 2 Graduate Program in Genetics, Stony Brook University, Stony Brook, New York, United States of America, 3 Medical Scientist Training Program, Stony Brook University, Stony Brook, New York, United States of America, 4 Department of Pharmacological Sciences, Stony Brook University, Stony Brook, New York, United States of America Abstract The mother centriole of the centrosome is distinguished from immature daughter centrioles by the presence of accessory structures (distal and subdistal appendages), which play an important role in the organization of the primary cilium in quiescent cells. Primary cilia serve as sensory organelles, thus have been implicated in mediating intracellular signal transduction pathways. Here we report that Chibby (Cby), a highly conserved antagonist of the Wnt/b-catenin pathway, is a centriolar component specifically located at the distal end of the mother centriole and essential for assembly of the primary cilium. Cby appeared as a discrete dot in the middle of a ring-like structure revealed by staining with a distal appendage component of Cep164. Cby interacted with one of the appendage components, Cenexin (Cnx), which thereby abrogated the inhibitory effect of Cby on b-catenin-mediated transcriptional activation in a dose-dependent manner. Cby a