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Sci Adv. 2020 Feb 14;6(7):eaaz4137. doi: 10.1126/sciadv.aaz4137. eCollection 2020 Feb.

A helical inner scaffold provides a structural basis for centriole cohesion.

Author information

1
University of Geneva, Department of Cell Biology, Sciences III, Geneva, Switzerland.
2
Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris Sud, Université Paris-Saclay, 1 Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
3
Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
4
Center for Cellular Imaging and NanoAnalytics (C-CINA), Biozentrum, University of Basel, Basel CH-4058, Switzerland.
5
Institut Curie, PSL Research University, CNRS-UMR 144, 75005 Paris, France.
6
Université de Paris, Institut Jacques Monod, CNRS UMR7592, 75013 Paris, France.
7
Helmholtz Pioneer Campus, Helmholtz Zentrum München, Ingolstädter Landstraße 1, 85764 Neuherberg, Germany.

Abstract

The ninefold radial arrangement of microtubule triplets (MTTs) is the hallmark of the centriole, a conserved organelle crucial for the formation of centrosomes and cilia. Although strong cohesion between MTTs is critical to resist forces applied by ciliary beating and the mitotic spindle, how the centriole maintains its structural integrity is not known. Using cryo-electron tomography and subtomogram averaging of centrioles from four evolutionarily distant species, we found that MTTs are bound together by a helical inner scaffold covering ~70% of the centriole length that maintains MTTs cohesion under compressive forces. Ultrastructure Expansion Microscopy (U-ExM) indicated that POC5, POC1B, FAM161A, and Centrin-2 localize to the scaffold structure along the inner wall of the centriole MTTs. Moreover, we established that these four proteins interact with each other to form a complex that binds microtubules. Together, our results provide a structural and molecular basis for centriole cohesion and geometry.

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