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

T. Tony Yang, Weng Man Chong, Won-Jing Wang, Gregory Mazo, Barbara Tanos, Zhengmin Chen, Thi Minh Nguyet Tran, Yi- De Chen, Rueyhung Roc Weng, Chia-En Huang, Wann-Neng Jane, Meng-Fu Bryan Tsou () and Jung-Chi Liao ()
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T. Tony Yang: Academia Sinica
Weng Man Chong: Academia Sinica
Won-Jing Wang: National Yang Ming University
Gregory Mazo: Memorial Sloan-Kettering Cancer Center
Barbara Tanos: Institute of Cancer Research
Zhengmin Chen: Academia Sinica
Thi Minh Nguyet Tran: Academia Sinica
Yi- De Chen: Academia Sinica
Rueyhung Roc Weng: Academia Sinica
Chia-En Huang: Academia Sinica
Wann-Neng Jane: Academia Sinica
Meng-Fu Bryan Tsou: Memorial Sloan-Kettering Cancer Center
Jung-Chi Liao: Academia Sinica

Nature Communications, 2018, vol. 9, issue 1, 1-11

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-04469-1

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