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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
More by this author
Institution:
University of Oxford
Division:
Societies, Other & Subsidiary Companies
Department:
Kellogg College
Oxford college:
Kellogg College
Role:
Author
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Name:
University of Exeter
Funding agency for:
Metz, J
Wakefield, J
Grant:
CLES Strategic Development Fund Award
More from this funder
Name:
Wellcome Trust
Funding agency for:
Chen, Z
Rappsiber, J
Grant:
108504
108504
More from this funder
Name:
Biotechnology and Biological Sciences Research Councils
Funding agency for:
Chen, J
Grant:
BB/K017837/1
More from this funder
Name:
University of Exeter / Taiwan President's PhD studentship
Funding agency for:
Chen, J
Grant:
BB/K017837/1
More from this funder
Name:
Engineering and Physical Sciences Research Council/ University of Oxford Systems Biology Doctoral Training Centre
Funding agency for:
Rogala, K
Publisher:
Company of Biologists
Journal:
Biology Open More from this journal
Volume:
2017
Issue:
6
Pages:
654-663
Publication date:
2017-03-28
Acceptance date:
2017-03-16
DOI:
ISSN:
2046-6390
Pubs id:
pubs:686667
UUID:
uuid:d113b251-554b-407e-918b-9fa9bd71d2d2
Local pid:
pubs:686667
Source identifiers:
686667
Deposit date:
2017-03-22

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