7FAD

Crystal structure of Xenopus GCP2-N terminal domain and Mzt2

Summary for 7FAD

• Entry DOI: 10.2210/pdb7fad/pdb
• Descriptor: Gamma-tubulin complex component, Mitotic-spindle organizing protein 2B (2 entities in total)
• Functional Keywords: microtubule nucleation, structural protein
• Biological source: Xenopus laevis (African clawed frog); More
• Total number of polymer chains: 6
• Total formula weight: 88157.24

Authors

Shankar, S.,Huang, T.L.,Hsia, K.C. (deposition date: 2021-07-06, release date: 2022-07-13, Last modification date: 2024-05-29)

Primary citation

Shankar, S.,Hsu, Z.T.,Ezquerra, A.,Li, C.C.,Huang, T.L.,Coyaud, E.,Viais, R.,Grauffel, C.,Raught, B.,Lim, C.,Luders, J.,Tsai, S.Y.,Hsia, K.C.
A gamma-tubulin complex independent pathway could suppress ciliogenesis by promoting cilia disassembly
Cell Rep, 41:111642-111642, 2022

PubMed 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.

PubMed: 36384111
DOI: 10.1016/j.celrep.2022.111642

Experimental method

X-RAY DIFFRACTION (3.204 Å)