TY - JOUR TI - Systematic studies of all PIH proteins in zebrafish reveal their distinct roles in axonemal dynein assembly AU - Yamaguchi, Hiroshi AU - Oda, Toshiyuki AU - Kikkawa, Masahide AU - Takeda, Hiroyuki A2 - Carter, Andrew P VL - 7 PY - 2018 DA - 2018/05/09 SP - e36979 C1 - eLife 2018;7:e36979 DO - 10.7554/eLife.36979 UR - https://doi.org/10.7554/eLife.36979 AB - Construction of motile cilia/flagella requires cytoplasmic preassembly of axonemal dyneins before transport into cilia. Axonemal dyneins have various subtypes, but the roles of each dynein subtype and their assembly processes remain elusive in vertebrates. The PIH protein family, consisting of four members, has been implicated in the assembly of different dynein subtypes, although evidence for this idea is sparse. Here, we established zebrafish mutants of all four PIH-protein genes: pih1d1, pih1d2, ktu, and twister, and analyzed the structures of axonemal dyneins in mutant spermatozoa by cryo-electron tomography. Mutations caused the loss of specific dynein subtypes, which was correlated with abnormal sperm motility. We also found organ-specific compositions of dynein subtypes, which could explain the severe motility defects of mutant Kupffer’s vesicle cilia. Our data demonstrate that all vertebrate PIH proteins are differently required for cilia/flagella motions and the assembly of axonemal dyneins, assigning specific dynein subtypes to each PIH protein. KW - cilia KW - axonemal dynein KW - cryo-electron tomography KW - sperm KW - zebrafish KW - PIH protein JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -