PXD071440-1

PXD071440 is an original dataset announced via ProteomeXchange.

Title	Dose-Dependent Inhibition of Protein Glycosylation Reveals Crosstalk Between Glycosylation and Phosphorylation in EGF Signaling Pathways
Description	Protein glycosylation and phosphorylation play critical roles in regulating diverse cellular processes, yet their interplay remains underexplored. This study employed a dose-dependent glycosylation inhibition to investigate the function of glycosylation, especially in phosphorylation in epidermal growth factor (EGF) signaling. Using quantitative proteomics, we analyzed global protein expression, glycopeptides, and phosphopeptides in EGF-stimulated and unstimulated conditions. Results revealed that glycosylation inhibition disrupted phosphorylation patterns in EGF-regulated pathways. Notably, 215 EGF-regulated phosphopeptides exhibited dose-dependent changes, with pathways such as ERBB, MAPK, and mTOR signaling being significantly affected. Protein-protein interaction analysis highlighted glycosylation-dependent modulation of phosphorylation in cytoskeletal remodeling and growth factor signaling. Correlation analysis identified site-specific glycopeptides, such as Asn568 of EGFR, that influenced phosphorylation of downstream signaling proteins. Additionally, individual proteins like RCN1 and SLC4A7 demonstrated glycosylation and phosphorylation regulated patterns. These findings underscored the role of glycosylation in maintaining phosphorylation-dependent signaling fidelity, providing insights into function of glycosylation on cell signaling pathways.
HostingRepository	PRIDE
AnnounceDate	2026-04-06
AnnouncementXML	Submission_2026-04-05_17:34:47.916.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Hongyi Liu
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606;
ModificationList	N-glycosylated residue; phosphorylated residue
Instrument	Orbitrap Ascend

Revision	Datetime	Status	ChangeLog Entry
0	2025-12-01 13:50:38	ID requested
⏵ 1	2026-04-05 17:34:48	announced

10.1021/acs.analchem.5c08113;

Liu H, Lin DC, Hu Y, Sun Z, Huang Y, Xu Y, Zhang H, Dose-Dependent Inhibition of Protein Glycosylation Reveals Crosstalk between Glycosylation and Phosphorylation in EGF Signaling Pathways. Anal Chem, 98(12):9293-9304(2026) [pubmed]

submitter keyword: tunicamycin,glycosylation, phosphorylation, proteomic, EGF

Hongyi Liu
contact affiliation	Johns Hopkins University
contact email	hliu173@jh.edu
lab head
Hongyi Liu
contact affiliation	Johns Hopkins University
contact email	hliu173@jh.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD071440
     1. Label: PRIDE project
     2. Name: Dose-Dependent Inhibition of Protein Glycosylation Reveals Crosstalk Between Glycosylation and Phosphorylation in EGF Signaling Pathways