Year: 2020
Type: article
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.
Source: Science Advances
Authors: Maeva Le Guennec, Nikolai Klena, Davide Gambarotto, Marine H. Laporte, Anne-Marie Tassin, Hugo van den Hoek, Philipp S. Erdmann, Miroslava Schaffer, Lubomir Kovacik, Susanne Borgers, Kenneth N. Goldie, Henning Stahlberg, Michel Bornens, Juliette Azimzadeh, Benjamin D. Engel, Virginie Hamel, Paul Guichard
Institutions: University of Geneva, Centre National de la Recherche Scientifique, Commissariat à l'Énergie Atomique et aux Énergies Alternatives, Université Paris-Saclay, Institut de Biologie Intégrative de la Cellule, Max Planck Institute of Biochemistry, University of Basel, Université Paris Sciences et Lettres, Biologie cellulaire et Cancer, Institut Curie, Université Paris Cité, Institut Jacques Monod, Helmholtz Munich
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $4,873
OpenAlex ID: W3006081271