Journal
SCIENCE ADVANCES
Volume 6, Issue 7, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.aaz4137
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Funding
- Swiss National Science Foundation (SNSF) [PP00P3_157517]
- European Research Council [ERC ACCENT StG 715289]
- French National Research Agency [ANR-15-CE11-0002-01]
- Max Planck Society
- Agence Nationale de la Recherche (ANR) [ANR-15-CE11-0002] Funding Source: Agence Nationale de la Recherche (ANR)
- Swiss National Science Foundation (SNF) [PP00P3_157517] Funding Source: Swiss National Science Foundation (SNF)
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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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