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Updated: May 28, 2026

Forming, Confining, and Observing Microtubule-Based Active Nematics
Published on: January 13, 2023
Microtubule nucleation by γ-tubulin complexes
Justin M Kollman1, Andreas Merdes, Lionel Mourey
1Howard Hughes Medical Institute and Department of Biochemistry & Biophysics, University of California, San Francisco, San Francisco, California 94143, USA.
Abstract:
Microtubule nucleation is regulated by the γ-tubulin ring complex (γTuRC) and related γ-tubulin complexes, providing spatial and temporal control over the initiation of microtubule growth. Recent structural work has shed light on the mechanism of γTuRC-based microtubule nucleation, confirming the long-standing hypothesis that the γTuRC functions as a microtubule template. The first crystallographic analysis of a non-γ-tubulin γTuRC component (γ-tubulin complex protein 4 (GCP4)) has resulted in a new appreciation of the relationships among all γTuRC proteins, leading to a refined model of their organization and function. The structures have also suggested an unexpected mechanism for regulating γTuRC activity via conformational modulation of the complex component GCP3. New experiments on γTuRC localization extend these insights, suggesting a direct link between its attachment at specific cellular sites and its activation.
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