PXD033167-2

PXD033167 is an original dataset announced via ProteomeXchange.

Title	Crosslinking-Mass Spectrometry data for structural analysis of Doublecortin-Microtubule interaction
Description	Doublecortin (DCX) is a microtubule (MT) associated protein that regulates MT structure and function during neuronal development and mutations in DCX lead to a spectrum of neurological disorders. The structural properties of MT-bound DCX remain poorly resolved. Here, we describe the molecular architecture of the DCX-MT complex through an integrative modeling approach that combines data from X-ray crystallography, cryo-EM and a high-fidelity chemical crosslinking method. We demonstrate that DCX interacts with MTs through its N-terminal domain and induces a lattice-dependent self-association involving both the C-terminal structured domain and the C-tails, in a conformation that favors an open, domain-swapped state. The networked state is shown to accommodate multiple different attachment points on the MT lattice, all of which orient the C-tails away from the lattice. As numerous disease mutations cluster in the C-terminus and regulatory phosphorylations cluster in the C-tail, our study shows that lattice-driven self-assembly is an important property of DCX.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:55:39.025.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Atefeh Rafiei
SpeciesList	scientific name: Sus scrofa domesticus (domestic pig); NCBI TaxID: 9825; scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2022-04-12 02:33:45	ID requested
1	2022-05-04 04:20:07	announced
⏵ 2	2023-11-14 08:55:39	announced	2023-11-14: Updated project metadata.

Dataset with its publication pending

submitter keyword: crosslinking-Mass spectrometry,Doublecortin, integrative structural modeling, Microtubule

David C. Schriemer
contact affiliation	Department of Biochemistry and Molecular Biology, University of Calgary, Alberta, Canada
contact email	dschriem@ucalgary.ca
lab head
Atefeh Rafiei
contact affiliation	University of Calgary
contact email	atefeh.rafiei@ucalgary.ca
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/2022/05/PXD033167

PRIDE project URI

• PRIDE
  1. PXD033167
     1. Label: PRIDE project
     2. Name: Crosslinking-Mass Spectrometry data for structural analysis of Doublecortin-Microtubule interaction