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The structure of the γ-TuRC at the microtubule minus end: not just one solution

In cells, microtubules (MTs) assemble from α/β-tubulin subunits at nucleation sites containing the γ-tubulin ring complex (γ-TuRC). Within the γ-TuRC, exposed γ-tubulin molecules act as templates for MT assembly by interacting with α/β-tubulin. The vertebrate γ-TuRC is scaffolded by γ-tubulin-intera...

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Main Authors: Gao, Qi (Author) , Vermeulen, Bram J. A. (Author) , Würtz, Martin (Author) , Shin, Hyesu (Author) , Erdogdu, Dilara (Author) , Zheng, Anjun (Author) , Hofer, Florian W. (Author) , Neuner, Annett (Author) , Pfeffer, Stefan (Author) , Schiebel, Elmar (Author)
Format: Article (Journal)
Language:English
Published: 23 July 2024
In: Bioessays
Year: 2024, Volume: 46, Issue: 9, Pages: 1-11
ISSN:1521-1878
DOI:10.1002/bies.202400117
Online Access:Verlag, kostenfrei, Volltext: https://doi.org/10.1002/bies.202400117
Verlag, kostenfrei, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1002/bies.202400117
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Author Notes:Qi Gao, Bram J. A. Vermeulen, Martin Würtz, Hyesu Shin, Dilara Erdogdu, Anjun Zheng, Florian W. Hofer, Annett Neuner, Stefan Pfeffer, Elmar Schiebel
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Summary:In cells, microtubules (MTs) assemble from α/β-tubulin subunits at nucleation sites containing the γ-tubulin ring complex (γ-TuRC). Within the γ-TuRC, exposed γ-tubulin molecules act as templates for MT assembly by interacting with α/β-tubulin. The vertebrate γ-TuRC is scaffolded by γ-tubulin-interacting proteins GCP2-6 arranged in a specific order. Interestingly, the γ-tubulin molecules in the γ-TuRC deviate from the cylindrical geometry of MTs, raising the question of how the γ-TuRC structure changes during MT nucleation. Recent studies on the structure of the vertebrate γ-TuRC attached to the end of MTs came to varying conclusions. In vitro assembly of MTs, facilitated by an α-tubulin mutant, resulted in a closed, cylindrical γ-TuRC showing canonical interactions between all γ-tubulin molecules and α/β-tubulin subunits. Conversely, native MTs formed in a frog extract were capped by a partially closed γ-TuRC, with some γ-tubulin molecules failing to align with α/β-tubulin. This review discusses these outcomes, along with the broader implications.
Item Description:Gesehen am 15.11.2024
Physical Description:Online Resource
ISSN:1521-1878
DOI:10.1002/bies.202400117

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