PXD040164

PXD040164 is an original dataset announced via ProteomeXchange.

Title	The C-terminal domain of periostin is intrinsically disordered and interacts with 143 proteins in an in vitro epidermal model of atopic dermatitis
Description	Human periostin is a 78-91 kDa alternatively spliced protein belonging to the group of matricellular proteins. The protein has been implicated in extracellular matrix remodeling, tumor development, and metastasis, inflammatory diseases like atopic dermatitis, psoriasis, and asthma. The C-terminal may be alternatively spliced, but the role of the ten variants is not understood. Here we investigate the structure of the C-terminal domain containing the protein sequence encoded by the fourall exons and its interactome. Structural analysis using SAXS, CD spectroscopy, and limited proteolysis suggested that the C-terminal domain was disordered. In addition, the motif responsible for heparin-binding was mapped to an arginine-rich sequence in the conserved very C-terminal part of periostin. Co-immunoprecipitationPull-down confirmed three known interaction partners bound to the C-terminal domain of periostin and identified an additional 140 novel potential interaction partners. Nine of these have been implicated in atopic dermatitis. Based on our findings, we suggest that the C-terminal domain anchor periostin to cell surfaces and facilitates interactions between connective tissue components or other cells. We propose that the C-terminal domain is a central part of the suggested function as a multifunctional modulator of extracellular matrix stability and wound healing.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_06:03:11.180.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD040164
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Christian Rusbjerg-Weberskov
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	iodoacetamide derivatized residue
Instrument	Orbitrap Eclipse

Revision	Datetime	Status	ChangeLog Entry
0	2023-02-16 09:51:35	ID requested
1	2023-09-15 03:12:12	announced
2	2023-11-14 09:05:12	announced	2023-11-14: Updated project metadata.
⏵ 3	2024-10-22 06:03:12	announced	2024-10-22: Updated project metadata.

10.1021/acs.biochem.3c00176;

Rusbjerg-Weberskov CE, Johansen ML, Nowak JS, Otzen DE, Pedersen JS, Enghild JJ, Nielsen NS, Periostin C-Terminal Is Intrinsically Disordered and Interacts with 143 Proteins in an In Vitro Epidermal Model of Atopic Dermatitis. Biochemistry, 62(19):2803-2815(2023) [pubmed]

10.6019/PXD040164;

submitter keyword: heparin-binding protein, extracellular matrix protein,periostin, wound healing, connective tissue, protein‐protein interactions, alternative splicing, intrinsically disordered protein, atopic dermatitis

Jan J. Enghild
contact affiliation	Institute of Molecular Biology and Genetics, Aarhus University, Denmark
contact email	jje@mbg.au.dk
lab head
Christian Rusbjerg-Weberskov
contact affiliation	Aarhus University
contact email	christianew@mbg.au.dk
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/2023/09/PXD040164

PRIDE project URI

• PRIDE
  1. PXD040164
     1. Label: PRIDE project
     2. Name: The C-terminal domain of periostin is intrinsically disordered and interacts with 143 proteins in an in vitro epidermal model of atopic dermatitis