Structure of the γ-tubulin ring complex-capped microtubule

Aher, Amol; Urnavicius, Linas; Xue, Allen; Neselu, Kasahun; Kapoor, Tarun M.

doi:10.1038/s41594-024-01264-z

Cited by 8 publications

(1 citation statement)

References 60 publications

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“…The γ-tubulin ring complex (γ-TuRC), for example, is the principal microtubule nucleation template that gives rise to canonical 13-protofilament microtubules. [61][62][63] For structural analysis, the low critical concentration of Xenopus tubulins (Figure 1D) allowed us to grow the microtubules in the absence of microtubule-stabilising agents or seeds. Therefore, the observed differences in architectural distribution (Figure 3D) must ultimately have arisen as a consequence of tubulin interactions specific for each Xenopus species.…”

Section: Discussionmentioning

confidence: 99%

Mechanistic basis of temperature-adaptation in microtubule dynamics across frog species

Troman,

de Gaulejac,

Biswas

et al. 2024

Preprint

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Cellular processes are remarkably effective across diverse temperature ranges, even with highly conserved proteins. In the context of the microtubule cytoskeleton, which is critically involved in a wide range of cellular activities, this is particularly striking as tubulin is one of the most conserved proteins while microtubule dynamic instability is highly temperature sensitive. We thus lack a mechanistic framework that links functional adaptability with environmental pressures. Here, we leverage the diversity of natural tubulin variants from three closely related frog species that live at different temperatures: we combine in vitro reconstitution assays, quantitative biochemistry, and cryogenic electron microscopy to show how a small number of primary sequence changes influences the energy landscape of tubulin interactions and thereby mediates cold-adaptation and microtubule stability. This study thus broadens our conceptual framework for understanding microtubule dynamics and provides insights into how conserved cellular processes are tailored to different ecological niches.

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Section: Discussionmentioning

confidence: 99%

Mechanistic basis of temperature-adaptation in microtubule dynamics across frog species

Troman,

de Gaulejac,

Biswas

et al. 2024

Preprint

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The structure of the γ‐TuRC at the microtubule minus end – not just one solution

Gao,

Vermeulen,

Würtz

et al. 2024

BioEssays

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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.

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CDK5RAP2 activates microtubule nucleator γTuRC by facilitating template formation and actin release

Serna,

Zimmermann,

Vineethakumari

et al. 2024

Developmental Cell

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Structure of the γ-tubulin ring complex-capped microtubule

Cited by 8 publications

References 60 publications

Mechanistic basis of temperature-adaptation in microtubule dynamics across frog species

Mechanistic basis of temperature-adaptation in microtubule dynamics across frog species

The structure of the γ‐TuRC at the microtubule minus end – not just one solution

CDK5RAP2 activates microtubule nucleator γTuRC by facilitating template formation and actin release

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