Α γ-tubulin complex-dependent pathway suppresses ciliogenesis by promoting cilia disassembly
Journal
Cell reports
Journal Volume
41
Journal Issue
7
Pages
111642
Date Issued
2022-11-15
Author(s)
Shankar, Sahana
Hsu, Zi-Ting
Ezquerra, Artur
Li, Chien-Chien
Huang, Tzu-Lun
Coyaud, Etienne
Viais, Ricardo
Grauffel, Cédric
Raught, Brian
Lim, Carmay
Lüders, Jens
Hsia, Kuo-Chiang
Abstract
The primary cilium, a microtubule-based sensory organelle, undergoes cycles of assembly and disassembly that govern the cell cycle progression critical to cell proliferation and differentiation. Although cilia assembly has been studied extensively, the molecular mechanisms underlying cilia disassembly are less well understood. Here, we uncover a γ-tubulin ring complex (γ-TuRC)-dependent pathway that promotes cilia disassembly and thereby prevents cilia formation. We further demonstrate that Kif2A, a kinesin motor that bears microtubule-depolymerizing activity, is recruited to the cilium basal body in a γ-TuRC-dependent manner. Our mechanistic analyses show that γ-TuRC specifically recruits Kif2A via the GCP2 subunit and its binding partner Mzt2. Hence, despite the long-standing view that γ-TuRC acts mainly as a microtubule template, we illustrate that its functional heterogeneity at the basal body facilitates both microtubule nucleation and Kif2A recruitment-mediated regulation of ciliogenesis, ensuring cell cycle progression.
Subjects
CP: Molecular biology; cell cycle; ciliogenesis; kinesin motor; microtubule; primary cilium; γ-tubulin ring complex
Publisher
Elsevier B.V.
Type
journal article