Cell-free reconstitution reveals synergistic stabilization of microtubule doublets by PACRG and FAP20
Abstract
Ciliary microtubule doublets, consisting of an incomplete B-tubule on the surface of a complete A-microtubule, form the fundamental structural framework of motile and sensory cilia/flagella. Ciliary proteins PACRG and FAP20, which are essential for flagellar stability and function, localize to the junction between the A- and the B-tubule. However, their precise role in microtubule doublet assembly and dynamics remains unknown. Here, using a cell-free assay, TIRF-microscopy, and cryo-electron tomography, we demonstrate that in combination PACRG and FAP20 stabilize B-tubule dynamics and microtubule doublet architecture. We show that together these proteins localize to the B-tubules in distinct, high-density patches, which locally stabilize B-tubule by decreasing its depolymerization velocity and increasing its rescue frequency. Cryo-tomography of in vitro reconstructed microtubule doublets in presence of PACRG and FAP20 reveals reduced B-tubule curvature fluctuations, promoting a more rigid and aligned conformation. Altogether, our findings suggest that PACRG and FAP20 function synergistically to reinforce microtubule doublet stability, ensuring ciliary integrity and function.
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BibTeX
@article{khuntsariya2026cellfree,
title = {{Cell-free reconstitution reveals synergistic stabilization of microtubule doublets by PACRG and FAP20}},
author = {Daria Khuntsariya and Umut Batman and Arya Krishnan and Souradip Mukherjee and Daniel Rozbesky and Florent Lemaitre and Carsten Janke and Virginie Hamel and Paul Guichard and Marcus Braun and Zdenek Lansky},
journal = {Nature Communications},
year = {2026},
month = oct,
doi = {10.1038/s41467-026-78500-1},
url = {https://www.nature.com/articles/s41467-026-78500-1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Cell-free reconstitution reveals synergistic stabilization of microtubule doublets by PACRG and FAP20
AU - Daria Khuntsariya
AU - Umut Batman
AU - Arya Krishnan
AU - Souradip Mukherjee
AU - Daniel Rozbesky
AU - Florent Lemaitre
AU - Carsten Janke
AU - Virginie Hamel
AU - Paul Guichard
AU - Marcus Braun
AU - Zdenek Lansky
PY - 2026
DA - 2026/10/16
JO - Nature Communications
DO - 10.1038/s41467-026-78500-1
UR - https://www.nature.com/articles/s41467-026-78500-1
AB - Ciliary microtubule doublets, consisting of an incomplete B-tubule on the surface of a complete A-microtubule, form the fundamental structural framework of motile and sensory cilia/flagella. Ciliary proteins PACRG and FAP20, which are essential for flagellar stability and function, localize to the junction between the A- and the B-tubule. However, their precise role in microtubule doublet assembly and dynamics remains unknown. Here, using a cell-free assay, TIRF-microscopy, and cryo-electron tomography, we demonstrate that in combination PACRG and FAP20 stabilize B-tubule dynamics and microtubule doublet architecture. We show that together these proteins localize to the B-tubules in distinct, high-density patches, which locally stabilize B-tubule by decreasing its depolymerization velocity and increasing its rescue frequency. Cryo-tomography of in vitro reconstructed microtubule doublets in presence of PACRG and FAP20 reveals reduced B-tubule curvature fluctuations, promoting a more rigid and aligned conformation. Altogether, our findings suggest that PACRG and FAP20 function synergistically to reinforce microtubule doublet stability, ensuring ciliary integrity and function.
SN - 2041-1723
ER -