Staged maturation converts a probasal body template complex into a nucleation-competent basal plate
- 1University of Warwick
Abstract
The central pair (CP) of microtubules is essential for flagellar motility, yet the molecular events underpinning its nucleation remain poorly defined. Here, we report a comprehensive screen of flagellar transition zone proteins that identifies new central pair assembly proteins (CPAPs). Using expansion microscopy, we reveal a concentric architecture at the basal plate, with themelin and basalin forming nested punctae with radial symmetry surrounding a central core containing TZP103.8, TZP48 and {gamma}-tubulin. A subset of CPAPs pre-assemble at the probasal body, a precursor structure that has not yet built a flagellum, with themelin functioning as the architectural template and master recruiter, and TZP103.8 and {gamma}-tubulin IFT-dependant addition being the final step of basal plate activation. Strikingly, in the absence of TZP103.8, {gamma}-tubulin still reaches the basal plate but is insufficient for central pair nucleation. We propose the staged assembly of CPAPs progressively constructs a structural template that geometrically constrains {gamma}-tubulin into the positions and orientations required for CP nucleation.
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BibTeX
@misc{paterou2026staged,
title = {{Staged maturation converts a probasal body template complex into a nucleation-competent basal plate}},
author = {A. Paterou and S. Dean},
howpublished = {bioRxiv},
year = {2026},
month = sep,
doi = {10.64898/2026.09.23.753794},
url = {https://www.biorxiv.org/content/10.64898/2026.09.23.753794v1},
note = {CC BY},
}
RIS
TY - UNPB
TI - Staged maturation converts a probasal body template complex into a nucleation-competent basal plate
AU - A. Paterou
AU - S. Dean
PY - 2026
DA - 2026/09/23
PB - bioRxiv
DO - 10.64898/2026.09.23.753794
UR - https://www.biorxiv.org/content/10.64898/2026.09.23.753794v1
AB - The central pair (CP) of microtubules is essential for flagellar motility, yet the molecular events underpinning its nucleation remain poorly defined. Here, we report a comprehensive screen of flagellar transition zone proteins that identifies new central pair assembly proteins (CPAPs). Using expansion microscopy, we reveal a concentric architecture at the basal plate, with themelin and basalin forming nested punctae with radial symmetry surrounding a central core containing TZP103.8, TZP48 and {gamma}-tubulin. A subset of CPAPs pre-assemble at the probasal body, a precursor structure that has not yet built a flagellum, with themelin functioning as the architectural template and master recruiter, and TZP103.8 and {gamma}-tubulin IFT-dependant addition being the final step of basal plate activation. Strikingly, in the absence of TZP103.8, {gamma}-tubulin still reaches the basal plate but is insufficient for central pair nucleation. We propose the staged assembly of CPAPs progressively constructs a structural template that geometrically constrains {gamma}-tubulin into the positions and orientations required for CP nucleation.
ER -