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Microtubule nucleation by γ-tubulin complexes

Nature Reviews Molecular Cell Biology volume 12, pages 709–721 (2011)Cite this article

Subjects

Key Points

  • The γ-tubulin small complex (γTuSC) alone can assemble into ring complexes with microtubule-like symmetry.

  • The structures of γ-tubulin complexes suggest that they serve as microtubule templates.

  • The γ-tubulin complex proteins (GCPs) are conserved in sequence, overall structure and their ability to bind γ-tubulin.

  • The conformation of the γTuSC may play a part in regulating its microtubule-nucleating activity.

  • A revised model of γ-tubulin ring complex (γTuRC) assembly, in which all of the GCPs are incorporated directly into the ring, has been proposed.

  • The attachment of the γTuRC to both centrosomal and non-centrosomal sites is linked to its activation.

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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Figure 1: Microtubule assembly.
Figure 2: The structure of γTuSC.
Figure 3: The GCP4 crystal structure defines the core structure of all of the GCPs.
Figure 4: A model for the conformational activation of the γTuSC.
Figure 5: A revised model of γTuRC assembly.
Figure 6: Modes of γTuSC- and γTuRC-specific attachment.

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Authors and Affiliations

  1. Howard Hughes Medical Institute and Department of Biochemistry & Biophysics, University of California, San Francisco, San Francisco, 94143, California, USA

    Justin M. Kollman & David A. Agard

  2. Centre de Recherche en Pharmacologie-Santé, Unité Mixte de Recherche 2587 Centre National de la Recherche Scientifique–Pierre Fabre, 31400, Toulouse, France

    Andreas Merdes

  3. Institut de Pharmacologie et de Biologie Structurale (IPBS), Centre National de la Recherche Scientifique (CNRS), and Université de Toulouse, Universit Paul Sabatier, IPBS, F-31077, Toulouse, France

    Lionel Mourey

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Glossary

Microtubule catastrophe

The rapid depolymerization of microtubules that occurs when GTP has been hydrolysed in all tubulin subunits up to the growing tip.

Microtubule-organizing centres

(MTOCs). Primary sites of microtubule nucleation in the cell, including centrosomes in animal cells and the spindle pole body in yeast.

Acentrosomal microtubule arrays

Ordered arrays of microtubules formed in the absence of a microtubule-organizing centre.

Chromosome-mediated nucleation

The pathway by which new microtubules are nucleated around chromosomes in response to a RAN gradient.

Deuterostome lineage

One of the two superphyla of more complex animals. It includes the echinoderms, chordates, hemichordates and xenoturbellida.

Single-particle electron microscopy

A method for combining two-dimensional images of molecules into a three-dimensional structure.

Normal mode analysis

A computational method for predicting the flexibility of a protein structure based on its shape.

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Kollman, J., Merdes, A., Mourey, L. et al. Microtubule nucleation by γ-tubulin complexes. Nat Rev Mol Cell Biol 12, 709–721 (2011). https://doi.org/10.1038/nrm3209

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