PXD062594-1
PXD062594 is an original dataset announced via ProteomeXchange.
Dataset Summary
| Title | O-mannose glycosylations influence E-cadherin protein interactions |
| Description | Cadherins are plasma membrane adhesion molecules that play critical roles in maintaining cell-cell adhesion and modulating cell signaling during development. Their functions are mediated by extracellular cadherin (EC) domains, which facilitate adhesive interactions and enable the formation of cis- and trans assemblies at adherens junctions and desmosomes. The EC domains adopt a characteristic immunoglobulin-like fold composed of seven beta-strands (A-G), and are further modified by N-linked and O-linked glycosylation, including alpha-linked mannose monosaccharides (O-Man) on conserved serine and threonine residues of B- and G-strands. EC domain O-Man glycosylation is catalyzed by TMTC enzymes: TMTC3 catalyzes modifications to the G-strands, whereas TMTC2 targets the B-strands. Given the site-specific deposition of O-Man glycans by dedicated enzymes and the central role of EC domains in cadherins functions, we hypothesized that these PTMs may fine-tune cellular adhesion strength and otherwise contribute to diverse physical interactions that involve cadherins. To test these hypotheses, we assayed for changes in protein-protein interactions formed with epithelial (E)-cadherin in model cells where O-Man PTMs were genetically ablated. Herein, we report O-Man-dependent, E-cadherin (CDH1) protein interactions, revealed by affinity proteomics; we orthogonally validate an altered association between CDH1 and CDH3 (P-cadherin), and demonstrate loss-of-function consequences of O-Man ablation on specific positions, highlighting the importance of these PTMs in cadherin-mediated adhesion. These findings provide new insights into how post-translational modifications regulate cadherin-dependent adhesion complexes. |
| HostingRepository | MassIVE |
| AnnounceDate | 2025-06-20 |
| AnnouncementXML | Submission_2025-06-20_10:00:39.601.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Non peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Shaoshuai Xie |
| SpeciesList | scientific name: Homo sapiens; common name: human; NCBI TaxID: 9606; |
| ModificationList | Label:13C(6)15N(4)+Methyl; Label:13C(6)15N(2)+Acetyl; Acetyl; Met-loss; Met-loss+Acetyl; L-cysteine methyl disulfide |
| Instrument | Orbitrap Exploris 480 |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
|---|---|---|---|
| 0 | 2025-04-04 02:40:44 | ID requested | |
| ⏵ 1 | 2025-06-20 10:00:39 | announced |
Publication List
| no publication |
Keyword List
| submitter keyword: E-cadherin interactome, IP screening, O-Man glycosyaltion, DatasetType:Proteomics |
Contact List
| John LaCava | |
|---|---|
| contact affiliation | Laboratory of Cellular and Structural Biology, The Rockefeller University |
| contact email | jlacava@rockefeller.edu |
| lab head | |
| Shaoshuai Xie | |
| contact affiliation | Shandong University |
| contact email | xieshaoshuai@hotmail.com |
| dataset submitter | |
Full Dataset Link List
| MassIVE dataset URI |
| 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://massive-ftp.ucsd.edu/v09/MSV000097524/ |
to receive all new ProteomeXchange dataset release announcements!
