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Cross-linking/mass spectrometry analysis of AUGMIN complex

ABSTRACT: We applied cross-linking/mass spectrometry to characterize in vivo Augmin from Drosophila in absence of any other structural information. The identified cross-links revealed topology of the Augmin complex and allowed us to predict potential interfaces between Augmin and γ-TuRC.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Drosophila Melanogaster (fruit Fly)

SUBMITTER: Zhuo Chen

LAB HEAD: Juri Rappsilber

PROVIDER: PXD006246 | Pride | 2017-04-04

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	Rappsilber_CLMS_AUGMIN_1.raw	Raw
	Rappsilber_CLMS_AUGMIN_2.raw	Raw
	Rappsilber_CLMS_AUGMIN_3.raw	Raw
	Rappsilber_CLMS_AUGMIN_PeakLists.zip	Other
	Rappsilber_CLMS_AUGMIN_SearchResults.csv	Csv

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Publications

Cross-linking mass spectrometry identifies new interfaces of Augmin required to localise the γ-tubulin ring complex to the mitotic spindle.

Chen Jack W C JWC Chen Zhuo A ZA Rogala Kacper B KB Metz Jeremy J Deane Charlotte M CM Rappsilber Juri J Wakefield James G JG

Biology open 20170515 5

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 ...[more]

PMID: 28351835

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