PXD071027 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | N-glycosylation of AXL receptor tyrosine kinase regulates its stability, phosphorylation and oncogenic function |
| Description | AXL, a receptor tyrosine kinase implicated in tumor progression, undergoes post-translational modifications that regulate its activity and stability. In this study, we have analyzed AXL immunoprecipitated from cell lines by liquid chromatography–tandem mass spectrometry (LC-MS/MS)-based glycoproteomics and show that AXL is extensively N-glycosylated in breast and ovarian cancer cells, existing predominantly as two isoforms corresponding to high-mannose and complex-type glycans. The extracellular cleaved soluble form of AXL (sAXL) primarily carries complex N-glycans. LC-MS/MS–based glycoproteomics analysis identified five glycosylation sites (Asn43, Asn157, Asn198, Asn339, and Asn345) with extensive microheterogeneity, including sialylation, fucosylation, and bisecting GlcNAc modifications. Overall, our results demonstrate that N-glycosylation is essential for AXL stability, localization, and oncogenic signaling, offering new insights into how glycosylation regulates receptor tyrosine kinases function in cancer. |
| HostingRepository | PRIDE |
| AnnounceDate | 2026-06-15 |
| AnnouncementXML | Submission_2026-06-14_16:59:37.701.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Xinyan Wu |
| SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606; |
| ModificationList | deamidated residue; iodoacetamide derivatized residue |
| Instrument | LTQ Orbitrap |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
|---|
| 0 | 2025-11-20 20:28:45 | ID requested | |
| ⏵ 1 | 2026-06-14 16:59:38 | announced | |
Publication List
| Wang L, Li L, Wang J, Garapati K, Li F, Khan MKH, Kong X, Bakshi H, Jiang D, Zheng S, Chen L, Yang J, Hou X, Kaufmann SH, Weroha SJ, Wang J, Pandey A, Wu X, N-Glycosylation of AXL Receptor Tyrosine Kinase Regulates Its Stability, Phosphorylation, and Oncogenic Function. Mol Cell Proteomics, 25(6):101574(2026) [pubmed] |
| 10.1016/j.mcpro.2026.101574; |
Keyword List
| submitter keyword: receptor tyrosine kinase, phosphorylation, AXL,N-glycosylation, proliferation |
Contact List
| Xinyan Wu |
|---|
| contact affiliation | Mayo Clinic |
| contact email | wu.xinyan@mayo.edu |
| lab head | |
| Xinyan Wu |
|---|
| contact affiliation | Mayo Clinic |
| contact email | wu.xinyan@mayo.edu |
| dataset submitter | |
Full Dataset Link List
Dataset FTP location
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| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD071027
- Label: PRIDE project
- Name: N-glycosylation of AXL receptor tyrosine kinase regulates its stability, phosphorylation and oncogenic function
