Super-resolution architecture of mammalian centriole distal appendages reveals distinct blade and matrix functional components
Journal
Nature Communications
Journal Volume
9
Journal Issue
1
Pages
263-275
Date Issued
2018
Author(s)
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.
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).
SDGs
Other Subjects
cell membrane protein; protein cep164; protein cep83; protein cep89; protein dap; protein fbf1; protein sclt1; protein sstr3; Smoothened protein; unclassified drug; cell cycle protein; CEP164 protein, human; CEP83 protein, human; CEP89 protein, human; FBF1 protein, human; microtubule associated protein; microtubule protein; SCLT1 protein, human; signal transducing adaptor protein; sodium channel; anatomy; electronic equipment; equipment component; mammal; matrix; membrane; nanoparticle; Article; cell membrane; centriole; cilium; distal appendage matrix; extracellular matrix; human; human cell; molecular docking; cell line; centriole; chemistry; cilium; CRISPR Cas system; epithelium cell; gene editing; gene expression; genetics; HEK293 cell line; metabolism; molecular imaging; protein multimerization; retinal pigment epithelium; ultrastructure; Mammalia; Adaptor Proteins, Signal Transducing; Cell Cycle Proteins; Cell Line; Centrioles; Cilia; CRISPR-Cas Systems; Epithelial Cells; Gene Editing; Gene Expression; HEK293 Cells; Humans; Microtubule Proteins; Microtubule-Associated Proteins; Molecular Imaging; Protein Multimerization; Retinal Pigment Epithelium; Sodium Channels
Publisher
Scopus
Type
journal article