Architecture of mammalian centriole distal appendages accommodates distinct blade and matrix functional elements

Yang, T. T.; Chong, W. M.; Wang, W.-J.; Mazo, G.; Tanos, B.; Chen, Z.; Tran, M. N. T.; Chen, Y.-D.; Weng, R. R.; Huang, C.-E.; Jane, W.-N.; Tsou, M.-F. B.; Liao, J.-C.

doi:10.1101/193474

bioRxiv · 10.1101/193474

Architecture of mammalian centriole distal appendages accommodates distinct blade and matrix functional elements

Yang, T. T.·Chong, W. M.·Wang, W.-J.·Mazo, G.·Tanos, B.·Chen, Z.·Tran, M. N. T.·Chen, Y.-D.·Weng, R. R.·Huang, C.-E.·Jane, W.-N.·Tsou, M.-F. B.·Liao, J.-C.

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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 determined a superresolved 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 termed 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.

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Yang, T. T., Chong, W. M., Wang, W.-J., Mazo, G., Tanos, B., Chen, Z., Tran, M. N. T., Chen, Y.-D., Weng, R. R., Huang, C.-E., Jane, W.-N., Tsou, M.-F. B., Liao, J.-C.. 2017-09-25. Architecture of mammalian centriole distal appendages accommodates distinct blade and matrix functional elements. https://doi.org/10.1101/193474

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