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. 2024 Apr 10;43(10):2062–2085. doi: 10.1038/s44318-024-00087-4

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. Creative Commons Public Domain Dedication waiver http://creativecommons.org/publicdomain/zero/1.0/ applies to the data associated with this article, unless otherwise stated in a credit line to the data, but does not extend to the graphical or creative elements of illustrations, charts, or figures. This waiver removes legal barriers to the re-use and mining of research data. According to standard scholarly practice, it is recommended to provide appropriate citation and attribution whenever technically possible.

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(A) The open γ-TuRC (dark grey curve) displays highly cooperative nucleation behaviour in response to α/β-tubulin concentration but has a low base rate of nucleation (Thawani et al, 2020). The fully closed γ-TuRC (light grey) has a high base rate of nucleation with a lack of cooperativity. A partially closed γ-TuRC (orange) would likely have an intermediate base rate of nucleation, while still retaining some cooperativity. Such behaviour could aid synergy of the γ-TuRC with α/β-tubulin-enriching factors. Graphs are for illustrative purposes and do not represent experimental or simulated data. (B) Misalignment between the γ-TuRC and MT protofilaments may promote release of freshly nucleated MTs from the γ-TuRC, e.g. by CAMSAP2 (red), and recycling of nucleation-competent γ-TuRC. Spoke 1 and 14 are coloured to highlight different degrees of γ-TuRC closure. Spoke numbers are indicated for spokes 1 and 14. Missing interactions around the protofilament at spoke 2 highlighted with red outlines. (C) Different activation cues may induce different degrees of γ-TuRC closure to accommodate differential requirements of nucleation rate and minus end stability. (D) The γ-TuRC may transiently visit a fully closed conformation that favours MT nucleation and subsequently relax to the partially closed conformation observed in our study to favour MT release.