PXD059644 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Identification of novel Kv1.3 channel-interacting proteins using proximity labelling in T-cells |
| Description | Potassium channels regulate membrane potential, calcium flux, cellular activation and effector functions of adaptive and innate immune cells. The voltage-activated Kv1.3 channel is an important regulator of T cell-mediated autoimmunity and microglia-mediated neuroinflammation. Kv1.3 channels, via protein-protein interactions, are localized with key immune proteins and pathways, allowing functional coupling between K+ efflux and immune mechanisms. To gain insights into proteins and pathways that interact with Kv1.3 channels, we applied a proximity-labeling proteomics approach to characterize protein interactors of the Kv1.3 channel in activated T cells. Biotin ligase TurboID was fused to either N or C termini of Kv1.3, stably expressed in Jurkat T cells and biotinylated proteins in proximity to Kv1.3 were enriched and quantified by mass spectrometry. We identified over 1,800 Kv1.3 interactors including known interactors (beta-integrins, Bax, Stat1) although majority were novel. We found that the N-terminus of Kv1.3 preferentially interacts with protein synthesis and protein trafficking machinery, while the C-terminus interacts with immune signaling and cell junction proteins. In contrast to Kv1.3 interactors in microglia, T cell Kv1.3 interactors included 182 cell surface, T cell receptor complex, mitochondrial, calcium sand cytokine-mediated signaling pathway and lymphocyte migration proteins. 178 Kv1.3 interactors in T cells also represent genetic risk factors of T cell-mediated autoimmunity, including STIM1, which was further validated using co-immunoprecipitation. Our studies reveal novel proteins and molecular pathways that interact with Kv1.3 channels in adaptive (T cell) and innate immune (microglia), providing a foundation for how Kv1.3 channels may regulate immune mechanisms in autoimmune and neurological diseases. |
| HostingRepository | PRIDE |
| AnnounceDate | 2026-03-23 |
| AnnouncementXML | Submission_2026-03-22_17:52:27.907.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | UPASNA SRIVASTAVA |
| SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606; |
| ModificationList | deamidated residue |
| Instrument | Q Exactive |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
| 0 | 2025-01-10 08:44:16 | ID requested | |
| ⏵ 1 | 2026-03-22 17:52:28 | announced | |
Publication List
| Kour D, Bowen CA, Srivastava U, Nguyen HM, Kumari R, Kumar P, Brandelli AD, Bitarafan S, Tobin BR, Wood LB, Seyfried NT, Wulff H, Rangaraju S, Identification of Novel Kv1.3 Channel-Interacting Proteins Using Proximity Labelling in T-Cells. Cell Physiol Biochem, 59(S1):41-70(2025) [pubmed] |
| 10.33594/000000823; |
Keyword List
| submitter keyword: autoimmune disease, T-cells, Potassium channel,Kv1.3 |
Contact List
| Upasna Srivastava |
| contact affiliation | Department of Neurology, School of Medicine, Yale University, New Haven (CT), USA |
| contact email | upasna.srivastava@yale.edu |
| lab head | |
| UPASNA SRIVASTAVA |
| contact affiliation | YALE UNIVERSITY |
| contact email | upasna.srivastava@yale.edu |
| 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/2026/03/PXD059644 |
| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD059644
- Label: PRIDE project
- Name: Identification of novel Kv1.3 channel-interacting proteins using proximity labelling in T-cells