Super-resolution architecture of mammalian centriole distal appendages reveals distinct blade and matrix functional components Journal Article


Authors: Yang, T. T.; Chong, W. M.; Wang, W. J.; Mazo, G.; Tanos, B.; Chen, Z.; Tran, T. M. N.; Chen, Y. D.; Weng, R. R.; Huang, C. E.; Jane, W. N.; Tsou, M. F. B.; Liao, J. C.
Article Title: Super-resolution architecture of mammalian centriole distal appendages reveals distinct blade and matrix functional components
Abstract: Distal appendages (DAPs) are nanoscale, pinwheel-like structures protruding from the distal end of the centriole that mediate membrane docking during ciliogenesis, marking the cilia base around the ciliary gate. Here we determine a super-resolved multiplex of 16 centriole-distal-end components. Surprisingly, rather than pinwheels, intact DAPs exhibit a cone-shaped architecture with components filling the space between each pinwheel blade, a new structural element we term the distal appendage matrix (DAM). Specifically, CEP83, CEP89, SCLT1, and CEP164 form the backbone of pinwheel blades, with CEP83 confined at the root and CEP164 extending to the tip near the membrane-docking site. By contrast, FBF1 marks the distal end of the DAM near the ciliary membrane. Strikingly, unlike CEP164, which is essential for ciliogenesis, FBF1 is required for ciliary gating of transmembrane proteins, revealing DAPs as an essential component of the ciliary gate. Our findings redefine both the structure and function of DAPs. © 2018 The Author(s).
Keywords: unclassified drug; human cell; mammalia; extracellular matrix; mammal; cell membrane; nanoparticle; anatomy; molecular docking; smoothened protein; centriole; membrane; matrix; cell membrane protein; human; article; cilium; protein cep164; protein cep83; protein cep89; protein dap; protein fbf1; protein sclt1; protein sstr3; electronic equipment; equipment component; distal appendage matrix
Journal Title: Nature Communications
Volume: 9
ISSN: 2041-1723
Publisher: Nature Publishing Group  
Date Published: 2018-05-22
Start Page: 2023
Language: English
DOI: 10.1038/s41467-018-04469-1
PROVIDER: scopus
PMCID: PMC5964178
PUBMED: 29789620
DOI/URL:
Notes: Article -- Export Date: 2 July 2018 -- Source: Scopus
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MSK Authors
  1. Meng-Fu Bryan Tsou
    28 Tsou
  2. Gregory   Mazo
    5 Mazo