PXD051853 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Biochemical basis of Exo70 specialization |
| Description | Molecular machines comprised by multiple subunits govern essential processes in the cell. Understanding how these complexes evolve is crucial to comprehend the evolution of cellular complexity. However, our understanding on the molecular mechanisms that allow multimeric complexes to change and acquire new functions is still limited. Here we used the plant exocyst complex as a model to study the evolution and mechanistic basis of neo-functionalization in multimeric protein complexes. By leveraging a combination of cell biology, proteomics, biochemistry, and phylogenetic analysis, we show the N-terminal domain of a single exocyst subunit, Exo70, have reverted its electrostatic charge over the course of evolution. This rendered a loose interaction with the rest of the complex and allowed Exo70 to rapidly diversify and acquire novel functions in plants. Our finding shows a novel model in which a single subunit scape from the evolutionary constrains of being in a complex, resulting in high diversification rates and neo-functionalization. |
| HostingRepository | PRIDE |
| AnnounceDate | 2025-12-01 |
| AnnouncementXML | Submission_2025-11-30_19:15:06.030.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Richard Imre |
| SpeciesList | scientific name: Marchantia polymorpha subsp. ruderalis; NCBI TaxID: NEWT:1480154; |
| ModificationList | methylthiolated residue; phosphorylated residue; monohydroxylated residue; deamidated residue |
| Instrument | Orbitrap Exploris 480 |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
|---|
| 0 | 2024-04-29 10:42:35 | ID requested | |
| ⏵ 1 | 2025-11-30 19:15:07 | announced | |
Publication List
| De la Concepcion JC, Duverge H, Kim Y, Julian J, Xu HD, Watt MN, Ikene SA, Bianchi A, Grujic N, Papareddy RK, Grishkovskaya I, Haselbach D, Murray DH, Clavel M, Irwin NAT, Dagdas Y, Electrostatic changes enabled the diversification of an exocyst subunit via protein complex escape. Nat Plants, 11(11):2350-2367(2025) [pubmed] |
| 10.1038/s41477-025-02135-1; |
Keyword List
| submitter keyword: Exocyst |
| Cell trafficking |
| evolution |
| Marchantia polymorpha |
| Biomolecular condensates |
| protein complexes. |
Contact List
| Yasin F. Dagdas |
|---|
| contact affiliation | Gregor Mendel Institute, Austrian Academy of Sciences, Vienna BioCenter, Vienna, Austria. |
| contact email | yasin.dagdas@gmi.oeaw.ac.at |
| lab head | |
| Richard Imre |
|---|
| contact affiliation | IMBA Vienna |
| contact email | richard.imre@imba.oeaw.ac.at |
| dataset submitter | |
Full Dataset Link List
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/2025/12/PXD051853 |
| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD051853
- Label: PRIDE project
- Name: Biochemical basis of Exo70 specialization
