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B21-High Throughput SAXS	Centriolar cap proteins CP110 and CPAP control slow elongation of microtubule plus ends Saishree S. Iyer , Fangrui Chen , Funso E. Ogunmolu , Shoeib Moradi , Vladimir A. Volkov , Emma J. Van Grinsven , Chris Van Hoorn , Jingchao Wu , Nemo Andrea , Shasha Hua , Kai Jiang , Ioannis Vakonakis , Mia Potočnjak , Franz Herzog , Benoît Gigant , Nikita Gudimchuk , Kelly E. Stecker , Marileen Dogterom , Michel O. Steinmetz , Anna Akhmanova Journal Of Cell Biology 224 DOI: 10.1083/jcb.202406061 Diamond Proposal Number(s): [21035] Open Access Show Abstract ▼ Abstract: Centrioles are microtubule-based organelles required for the formation of centrosomes and cilia. Centriolar microtubules, unlike their cytosolic counterparts, are stable and grow very slowly, but the underlying mechanisms are poorly understood. Here, we reconstituted in vitro the interplay between the proteins that cap distal centriole ends and control their elongation: CP110, CEP97, and CPAP/SAS-4. We found that whereas CEP97 does not bind to microtubules directly, CP110 autonomously binds microtubule plus ends, blocks their growth, and inhibits depolymerization. Cryo-electron tomography revealed that CP110 associates with the luminal side of microtubule plus ends and suppresses protofilament flaring. CP110 directly interacts with CPAP, which acts as a microtubule polymerase that overcomes CP110-induced growth inhibition. Together, the two proteins impose extremely slow processive microtubule growth. Disruption of CP110–CPAP interaction in cells inhibits centriole elongation and increases incidence of centriole defects. Our findings reveal how two centriolar cap proteins with opposing activities regulate microtubule plus-end elongation and explain their antagonistic relationship during centriole formation.	Mar 2025

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B21-High Throughput SAXS

Centriolar cap proteins CP110 and CPAP control slow elongation of microtubule plus ends