A stable microtubule bundle formed through an orchestrated multistep process controls quiescence exit

Autor: Damien Laporte, Aurelie Massoni-Laporte, Charles Lefranc, Jim Dompierre, David Mauboules, Emmanuel T Nsamba, Anne Royou, Lihi Gal, Maya Schuldiner, Mohan L Gupta, Isabelle Sagot
Jazyk: angličtina
Rok vydání: 2024
Předmět:
Zdroj: eLife, Vol 12 (2024)
Druh dokumentu: article
ISSN: 2050-084X
DOI: 10.7554/eLife.89958
Popis: Cells fine-tune microtubule assembly in both space and time to give rise to distinct edifices with specific cellular functions. In proliferating cells, microtubules are highly dynamics, and proliferation cessation often leads to their stabilization. One of the most stable microtubule structures identified to date is the nuclear bundle assembled in quiescent yeast. In this article, we characterize the original multistep process driving the assembly of this structure. This Aurora B-dependent mechanism follows a precise temporality that relies on the sequential actions of kinesin-14, kinesin-5, and involves both microtubule–kinetochore and kinetochore–kinetochore interactions. Upon quiescence exit, the microtubule bundle is disassembled via a cooperative process involving kinesin-8 and its full disassembly is required prior to cells re-entry into proliferation. Overall, our study provides the first description, at the molecular scale, of the entire life cycle of a stable microtubule structure in vivo and sheds light on its physiological function.
Databáze: Directory of Open Access Journals