PXD034895

PXD034895 is an original dataset announced via ProteomeXchange.

Title	The augmin complex architecture reveals structural insights into microtubule branching
Description	In mitosis, the augmin complex binds to spindle microtubules to recruit the γ-tubulin ring complex (γ-TuRC), the principal microtubule nucleator, for the formation of branched microtubules. Our understanding of augmin-mediated microtubule branching is strongly hampered by the lack of structural information on the augmin complex. Here we elucidate the molecular architecture and define the conformational plasticity of the augmin complex using an integrative structural biology approach. The elongated structure of the augmin complex is characterised by extensive coiled-coil segments and comprises two structural elements with distinct but complementary functions in γ-TuRC and microtubule binding, linked by a flexible hinge. The augmin complex is recruited to microtubules via a composite microtubule binding site comprising a positively charged unordered extension and two Calponin homology domains. Our study provides the structural basis for augmin function in branched microtubule formation, decisively fostering our understanding of spindle formation in mitosis.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_07:14:29.494.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Erik Zupa
SpeciesList	scientific name: Xenopus laevis (African clawed frog); NCBI TaxID: 8355;
ModificationList	acetylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2022-06-26 07:29:00	ID requested
1	2022-10-13 03:51:13	announced
⏵ 2	2023-11-14 07:14:30	announced	2023-11-14: Updated project metadata.

Zupa E, W, ü, rtz M, Neuner A, Hoffmann T, Rettel M, B, ö, hler A, Vermeulen BJA, Eustermann S, Schiebel E, Pfeffer S, The augmin complex architecture reveals structural insights into microtubule branching. Nat Commun, 13(1):5635(2022) [pubmed]

submitter keyword: microtubule, augmin, nucleation, cell cycle, branching

Stefan Pfeffer
contact affiliation	Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany
contact email	s.pfeffer@zmbh.uni-heidelberg.de
lab head
Erik Zupa
contact affiliation	Heidelberg University
contact email	e.zupa@zmbh.uni-heidelberg.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/10/PXD034895

PRIDE project URI

• PRIDE
  1. PXD034895
     1. Label: PRIDE project
     2. Name: The augmin complex architecture reveals structural insights into microtubule branching