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

• Published in: Nature communications Vol. 9; no. 1; pp. 2023 - 11
• Main Authors: Yang, T. Tony, Chong, Weng Man, Wang, Won-Jing, Mazo, Gregory, Tanos, Barbara, Chen, Zhengmin, Tran, Thi Minh Nguyet, Chen, Yi-De, Weng, Rueyhung Roc, Huang, Chia-En, Jane, Wann-Neng, Tsou, Meng-Fu Bryan, Liao, Jung-Chi
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 22.05.2018; Nature Publishing Group; Nature Portfolio
• Subjects: 13/109; 13/89; 14/63; 147/143; 631/136/2432; 631/80/128/1383; 631/80/128/1965; Adaptor Proteins, Signal Transducing - chemistry; Adaptor Proteins, Signal Transducing - genetics; Adaptor Proteins, Signal Transducing - metabolism; Appendages; Architecture; Biology; Cell cycle; Cell Cycle Proteins - genetics; Cell Cycle Proteins - metabolism; Cell Cycle Proteins - ultrastructure; Cell Line; Centrioles - metabolism; Centrioles - ultrastructure; Cilia; Cilia - metabolism; Cilia - ultrastructure; CRISPR-Cas Systems; Docking; Epithelial Cells - metabolism; Epithelial Cells - ultrastructure; Gating; Gene Editing; Gene Expression; HEK293 Cells; Humanities and Social Sciences; Humans; Localization; Membrane proteins; Microscopy; Microtubule Proteins - genetics; Microtubule Proteins - metabolism; Microtubule Proteins - ultrastructure; Microtubule-Associated Proteins - genetics; Microtubule-Associated Proteins - metabolism; Microtubule-Associated Proteins - ultrastructure; Molecular Imaging; multidisciplinary; Protein Multimerization; Proteins; Retinal Pigment Epithelium - metabolism; Retinal Pigment Epithelium - ultrastructure; Science; Science (multidisciplinary); Sodium Channels - genetics; Sodium Channels - metabolism; Sodium Channels - ultrastructure; Structure-function relationships
• ISSN: 2041-1723; 2041-1723
• DOI: 10.1038/s41467-018-04469-1

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. Distal appendages (DAPs) at the cilia base mediate membrane docking during ciliogenesis. Here the authors use super-resolution microscopy to map 16 centriole distal end components, revealing the structure of the backbone of the DAP, as well as a previously undescribed distal appendage matrix.