The Mn-motif protein MAP6d1 assembles ciliary doublet microtubules

Dharshini Gopal, Juliette Wu, Julie Delaroche, Christophe Bosc, Manon Andrade, Eric Denarier, Gregory Effantin, Annie Andrieux, Sylvie Gory-Fauré (), Laurence Serre () and Isabelle Arnal ()
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Dharshini Gopal: Université Grenoble Alpes
Juliette Wu: Université Grenoble Alpes
Julie Delaroche: Université Grenoble Alpes
Christophe Bosc: Université Grenoble Alpes
Manon Andrade: Université Grenoble Alpes
Eric Denarier: Université Grenoble Alpes
Gregory Effantin: Université Grenoble Alpes
Annie Andrieux: Université Grenoble Alpes
Sylvie Gory-Fauré: Université Grenoble Alpes
Laurence Serre: Université Grenoble Alpes
Isabelle Arnal: Université Grenoble Alpes

Nature Communications, 2025, vol. 16, issue 1, 1-15

Abstract: Abstract Most eukaryotic cells have cilia that serve vital functions in sensing, signalling, motility. The core architecture of cilia is an array of microtubule doublets, which consist of a complete A-tubule and an incomplete B-tubule. How these structures assemble remains poorly understood. Using total internal reflection fluorescence microscopy and cryo-electron tomography, we investigate the role of MAP6d1, a brain-specific protein containing microtubule lumen-targeting Mn-motifs. We show that MAP6d1 assembles stable microtubule doublets by recruiting tubulin dimers onto the A-tubule lattice to initiate B-tubule nucleation. MAP6d1 also promotes the formation of luminal protofilaments in singlet and doublet microtubules, a previously undescribed phenomenon that likely enhances microtubule stability. In neurons, MAP6d1 localises to the proximal part of primary cilia via its Mn-motif, with its loss resulting in shortened cilia, a characteristic of ciliopathies. MAP6d1 is thus a neuronal Mn-motif protein with a specific role in assembling microtubule doublets and regulating ciliary length.

Date: 2025
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DOI: 10.1038/s41467-025-61679-0

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