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Cross-linking mass spectrometry identifies new interfaces of Augmin required to localise the γ-Tubulin Ring Complex to the mitotic spindle

Abstract:

The hetero-octameric protein complex, Augmin, recruits γ-Tubulin Ring Complex (γ-TuRC) to pre-existing microtubules (MTs) to generate branched MTs during mitosis, facilitating robust spindle assembly. However, despite a recent partial reconstitution of the human Augmin complex in vitro, the molecular basis of this recruitment remains unclear. Here, we used immuno-affinity purification of in vivo Augmin from Drosophila and cross-linking/mass spectrometry to identify distance restraints between...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1242/bio.022905

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Institution:
University of Oxford
Division:
MPLS
Department:
Statistics
Role:
Author
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Institution:
University of Oxford
Division:
Societies, Other & Subsidiary Companies
Department:
Kellogg College
Oxford college:
Kellogg College
Role:
Author
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More from this funder
Funding agency for:
Chen, Z
Grant:
108504
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Publisher:
Company of Biologists Publisher's website
Journal:
Biology Open Journal website
Volume:
2017
Issue:
6
Pages:
654-663
Publication date:
2017-03-28
Acceptance date:
2017-03-16
DOI:
ISSN:
2046-6390
Source identifiers:
686667
Pubs id:
pubs:686667
UUID:
uuid:d113b251-554b-407e-918b-9fa9bd71d2d2
Local pid:
pubs:686667
Deposit date:
2017-03-22

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