PXD071027

PXD071027 is an original dataset announced via ProteomeXchange.

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

Revision	Datetime	Status	ChangeLog Entry
0	2025-11-20 20:28:45	ID requested
⏵ 1	2026-06-14 16:59:38	announced

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;

submitter keyword: receptor tyrosine kinase, phosphorylation, AXL,N-glycosylation, proliferation

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

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/2026/06/PXD071027

PRIDE project URI

• PRIDE
  1. PXD071027
     1. Label: PRIDE project
     2. Name: N-glycosylation of AXL receptor tyrosine kinase regulates its stability, phosphorylation and oncogenic function