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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Yang TT,Chong WM,Wang WJ,Mazo G,Tanos B,Chen Z,Tran TMN,Chen YD,Weng RR,Huang CE,Jane WN,Tsou MB,Liao JCdoi
10.1038/s41467-018-04469-1subject
Has Abstractpub_date
2018-05-22 00:00:00pages
2023issue
1issn
2041-1723pii
10.1038/s41467-018-04469-1journal_volume
9pub_type
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