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Mechanism of how augmin directly targets the γ-tubulin ring complex to microtubules

Microtubules (MTs) must be generated from precise locations to form the structural frameworks required for cell shape and function. MTs are nucleated by the γ-tubulin ring complex (γ-TuRC), but it remains unclear how γ-TuRC gets to the right location. Augmin has been suggested to be a γ-TuRC targeti...

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Autores principales: Song, Jae-Geun, King, Matthew R., Zhang, Rui, Kadzik, Rachel S., Thawani, Akanksha, Petry, Sabine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Rockefeller University Press 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6028527/
https://www.ncbi.nlm.nih.gov/pubmed/29875259
http://dx.doi.org/10.1083/jcb.201711090
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author Song, Jae-Geun
King, Matthew R.
Zhang, Rui
Kadzik, Rachel S.
Thawani, Akanksha
Petry, Sabine
author_facet Song, Jae-Geun
King, Matthew R.
Zhang, Rui
Kadzik, Rachel S.
Thawani, Akanksha
Petry, Sabine
author_sort Song, Jae-Geun
collection PubMed
description Microtubules (MTs) must be generated from precise locations to form the structural frameworks required for cell shape and function. MTs are nucleated by the γ-tubulin ring complex (γ-TuRC), but it remains unclear how γ-TuRC gets to the right location. Augmin has been suggested to be a γ-TuRC targeting factor and is required for MT nucleation from preexisting MTs. To determine augmin’s architecture and function, we purified Xenopus laevis augmin from insect cells. We demonstrate that augmin is sufficient to target γ-TuRC to MTs by in vitro reconstitution. Augmin is composed of two functional parts. One module (tetramer-II) is necessary for MT binding, whereas the other (tetramer-III) interacts with γ-TuRC. Negative-stain electron microscopy reveals that both tetramers fit into the Y-shape of augmin, and MT branching assays reveal that both are necessary for MT nucleation. The finding that augmin can directly bridge MTs with γ-TuRC via these two tetramers adds to our mechanistic understanding of how MTs can be nucleated from preexisting MTs.
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spelling pubmed-60285272019-01-02 Mechanism of how augmin directly targets the γ-tubulin ring complex to microtubules Song, Jae-Geun King, Matthew R. Zhang, Rui Kadzik, Rachel S. Thawani, Akanksha Petry, Sabine J Cell Biol Research Articles Microtubules (MTs) must be generated from precise locations to form the structural frameworks required for cell shape and function. MTs are nucleated by the γ-tubulin ring complex (γ-TuRC), but it remains unclear how γ-TuRC gets to the right location. Augmin has been suggested to be a γ-TuRC targeting factor and is required for MT nucleation from preexisting MTs. To determine augmin’s architecture and function, we purified Xenopus laevis augmin from insect cells. We demonstrate that augmin is sufficient to target γ-TuRC to MTs by in vitro reconstitution. Augmin is composed of two functional parts. One module (tetramer-II) is necessary for MT binding, whereas the other (tetramer-III) interacts with γ-TuRC. Negative-stain electron microscopy reveals that both tetramers fit into the Y-shape of augmin, and MT branching assays reveal that both are necessary for MT nucleation. The finding that augmin can directly bridge MTs with γ-TuRC via these two tetramers adds to our mechanistic understanding of how MTs can be nucleated from preexisting MTs. Rockefeller University Press 2018-07-02 /pmc/articles/PMC6028527/ /pubmed/29875259 http://dx.doi.org/10.1083/jcb.201711090 Text en © 2018 Song et al. http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Research Articles
Song, Jae-Geun
King, Matthew R.
Zhang, Rui
Kadzik, Rachel S.
Thawani, Akanksha
Petry, Sabine
Mechanism of how augmin directly targets the γ-tubulin ring complex to microtubules
title Mechanism of how augmin directly targets the γ-tubulin ring complex to microtubules
title_full Mechanism of how augmin directly targets the γ-tubulin ring complex to microtubules
title_fullStr Mechanism of how augmin directly targets the γ-tubulin ring complex to microtubules
title_full_unstemmed Mechanism of how augmin directly targets the γ-tubulin ring complex to microtubules
title_short Mechanism of how augmin directly targets the γ-tubulin ring complex to microtubules
title_sort mechanism of how augmin directly targets the γ-tubulin ring complex to microtubules
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6028527/
https://www.ncbi.nlm.nih.gov/pubmed/29875259
http://dx.doi.org/10.1083/jcb.201711090
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