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A helical inner scaffold provides a structural basis for centriole cohesion.
Sci. Adv. 6:eaaz4137 (2020)
Postprint
Forschungsdaten
DOI
PMC
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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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
Basal Bodies; De-novo; Protein; Architecture; Visualization; Purification; Centrosomes; Disruption; Fam161a; Poc1
ISSN (print) / ISBN
2375-2548
e-ISSN
2375-2548
Zeitschrift
Science Advances
Quellenangaben
Band: 6,
Heft: 7,
Artikelnummer: eaaz4137
Verlag
American Association for the Advancement of Science (AAAS)
Verlagsort
Washington, DC [u.a.]
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Helmholtz Pioneer Campus (HPC)