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Microtubule nucleation by γ-tubulin complexes
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Microtubule nucleation by γ-tubulin complexes
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Journal Article
Microtubule nucleation by γ-tubulin complexes
2011
Overview
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.
Microtubule nucleation is regulated by the γ-tubulin small complex (γTuSC) and the γ-tubulin ring complex (γTuRC). Recent structural work, including the crystallographic analysis of γ-tubulin complex protein 4 (GCP4), provides new insights into the mechanism of γTuRC-based microtubule nucleation, confirming the hypothesis that the γTuRC functions as a microtubule template.
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.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Animals
/ Biochemistry, Molecular Biology
/ Biomedical and Life Sciences
/ Cellular signal transduction
/ Humans
/ Microtubule-Associated Proteins - chemistry
/ Microtubule-Associated Proteins - physiology
/ Microtubule-Associated Proteins - ultrastructure
/ Microtubules - ultrastructure
/ Multiprotein Complexes - chemistry
/ Multiprotein Complexes - ultrastructure
