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Le Guennec, M.* ; Klena, N.* ; Gambarotto, D.* ; Laporte, M.H.* ; Tassin, A.M.* ; van den Hoek, H.* ; Erdmann, P.S.* ; Schaffer, M.* ; Kovacik, L.* ; Borgers, S.* ; Goldie, K.N.* ; Stahlberg, H.* ; Bornens, M.* ; Azimzadeh, J.* ; Engel, B.D. ; Hamel, V.* ; Guichard, P.*

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

Sci. Adv. 6:eaaz4137 (2020)
Publ. Version/Full Text Research data DOI
Open Access Gold
Creative Commons Lizenzvertrag
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 similar to 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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Publication type Article: Journal article
Document type Scientific Article
Keywords Basal Bodies; De-novo; Protein; Architecture; Visualization; Purification; Centrosomes; Disruption; Fam161a; Poc1
ISSN (print) / ISBN 2375-2548
e-ISSN 2375-2548
Quellenangaben Volume: 6, Issue: 7, Pages: , Article Number: eaaz4137 Supplement: ,
Publisher American Association for the Advancement of Science (AAAS)
Publishing Place Washington, DC [u.a.]
Reviewing status Peer reviewed
Institute(s) Helmholtz Pioneer Campus (HPC)