Graduate School of Frontier Biosciences, Osaka University


Pih1d3 is required for cytoplasmic preassembly of axonemal dynein in mouse sperm

Journal J Cell Biol 204, 203-213 (2014)
Authors Fenglan Dong (1), Kyosuke Shinohara (1), Yanick Botilde (1), Ryo Nabeshima (1), Yasuko Asai (1), Akemi Fukumoto (1), Toshiaki Hasegawa (2), Moe Matsuo (3), Hiroyuki Takeda (3), Hidetaka Shiratori (1), Tetsuya Nakamura (1), and Hiroshi Hamada (1)

  1. Developmental Genetics Group, Graduate School of Frontier Biosciences, Osaka University, and Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Corporation (JST), 1-3 Yamada-oka, Suita, Osaka 565-0871, Japan
  2. Research Center for Ultrahigh Voltage Electron Microscopy, Osaka University, 7-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan
  3. Department of Biological Sciences, Graduate School of Science, University of Tokyo, 7-3-1 Hongoh, Bunkyo-ku, Tokyo 113-0033, Japan
Title Pih1d3 is required for cytoplasmic preassembly of axonemal dynein in mouse sperm
PubMed 24421334
Description Axonemal dynein complexes are preassembled in the cytoplasm before their transport to cilia, but the mechanism of this process remains unclear. We now show that mice lacking Pih1d3, a PIH1 domain-containing protein, develop normally but manifest male sterility. Pih1d3(-/-) sperm were immotile and fragile, with the axoneme of the flagellum lacking outer dynein arms (ODAs) and inner dynein arms (IDAs) and showing a disturbed 9+2 microtubule organization. Pih1d3 was expressed specifically in spermatogenic cells, with the mRNA being most abundant in pachytene spermatocytes. Pih1d3 localized to the cytoplasm of spermatogenic cells but was not detected in spermatids or mature sperm. The levels of ODA and IDA proteins were reduced in the mutant testis and sperm, and Pih1d3 was found to interact with an intermediate chain of ODA as well as with Hsp70 and Hsp90. Our results suggest that Pih1d3 contributes to cytoplasmic preassembly of dynein complexes in spermatogenic cells by stabilizing and promoting complex formation by ODA and IDA proteins.