Unveiling the intriguing role of FAP20 in tubulin recruitment at the doublet microtubule inner junctions

Corbin S Black; Khanh Huy Bui

doi:10.1016/j.str.2023.11.004

Unveiling the intriguing role of FAP20 in tubulin recruitment at the doublet microtubule inner junctions

Structure. 2023 Dec 7;31(12):1518-1519. doi: 10.1016/j.str.2023.11.004.

Authors

Corbin S Black¹, Khanh Huy Bui²

Affiliations

¹ Facility for Electron Microscopy Research, McGill University, Montreal, QC, Canada. Electronic address: corbin.black@mcgill.ca.
² Department of Anatomy and Cell Biology, McGill University, Montreal, QC, Canada. Electronic address: huy.bui@mcgill.ca.

PMID: 38065073
DOI: 10.1016/j.str.2023.11.004

Abstract

In this issue of Structure, Bangera et al. investigate the role of the inner junction protein FAP20 in doublet microtubule assembly. Using cryo-EM and microtubule dynamic assays, they demonstrate that FAP20 recruits free tubulins to existing microtubule lattices, shedding light on B-tubule closure during doublet microtubule formation.

Publication types

Comment

MeSH terms

Axoneme / metabolism
Cilia / metabolism
Flagella* / metabolism
Microtubules / metabolism
Tubulin* / metabolism

Substances

Tubulin