PXD043485
PXD043485 is an original dataset announced via ProteomeXchange.
Dataset Summary
Title | Spatially resolved profiling of protein conformation and interactions by biocompatible chemical cross-linking in living cells |
Description | The protein structures and interactions that maintain and regulate cellular processes in different subcellular organelles are heterogeneous and dynamic. However, it remains challenging to characterize the subcellular specificity and translocation of protein complexes in terms of conformation and interactions. Herein, we developed a spatially resolved protein complex profiling approach by biocompatible chemical cross-linking in living cells (SPACX) to monitor the dynamics of protein conformation, interactions and translocation. The advancement of fast capturing protein complexes in the physiological state, coupled with efficient enrichment of the cross-linked peptides, ensured deep-coverage analysis of the protein interactome in living cells. By ensemble structure refinement with cross-linking restraints, subcellular-specific conformation heterogeneity was identified for PTEN. PTEN displayed a broader range of dynamic conformation changes on the dual specificity domains in the nucleus than in the cytoplasm. Moreover, based on conformational differences, different interacting assemblies involving 128 cytoplasm-exclusively and 237 nucleus-exclusively PTEN-interacting proteins were found to account for diverse biological functions. Upon ubiquitin-proteasome system (UPS) stress, the assembly of PTEN and its interacting partners changed obviously during translocation. Both the components and interacting sites were dynamically identified in-vivo by SPACX approach coupled with subcellular isolation, and the corresponding functional pathways were highly enriched. Inspiringly, the distinguished interacting proteins among isoforms of PTEN and PTEN-L were accessible by the determination of sequence-unique cross-linking interfaces for direct interactions. All these results indicate the promise of SPACX to elucidate the functional heterogeneity of proteins in individual subcellular sociology. |
HostingRepository | jPOST |
AnnounceDate | 2024-07-02 |
AnnouncementXML | Submission_2024-07-01_08:00:04.974.xml |
DigitalObjectIdentifier | |
ReviewLevel | Non peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Lili Zhao |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; scientific name: cellular organisms; NCBI TaxID: 131567; scientific name: Escherichia coli; NCBI TaxID: 562; |
ModificationList | S-carboxamidomethyl-L-cysteine; alpha-amino acetylated residue; L-methionine sulfoxide |
Instrument | LTQ Orbitrap; Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
---|---|---|---|
0 | 2023-07-03 04:47:58 | ID requested | |
⏵ 1 | 2024-07-01 08:00:05 | announced |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: LC-MS/MS, cross-linking |
Contact List
Lihua Zhang | |
---|---|
lab head | |
Lili Zhao | |
contact affiliation | DICP |
dataset submitter |
Full Dataset Link List
jPOST 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://ftp.jpostdb.org/JPST002231/ |