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Systematic Quantification of Protein O-GlcNAcylation Reveals Common and Cell-Type-Specific Responses to N-Glycosylation Inhibition in Human Cells

ABSTRACT: In this work, we systematically and site-specifically analyzed protein O-GlcNAcylation under the N-glycosylation inhibition through the integration of metabolic labeling, bio-orthogonal chemistry, and multiplexed proteomics. The experiments were performed in three types of human cells, i.e., HEK293T, HepG2, and Jurkat cells.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): T Cell

DISEASE(S): Liver Cancer

SUBMITTER: Longping Fu

LAB HEAD: Ronghu Wu

PROVIDER: PXD073249 | Pride | 2026-06-02

REPOSITORIES: Pride

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			Action	DRS
	Eclipse_LF_OGlycoTM_HEK293T_OG_10_10062025.raw	Raw
	Eclipse_LF_OGlycoTM_HEK293T_OG_11_10062025.raw	Raw
	Eclipse_LF_OGlycoTM_HEK293T_OG_12_10062025.raw	Raw
	Eclipse_LF_OGlycoTM_HEK293T_OG_13_10062025_20251028210557.raw	Raw
	Eclipse_LF_OGlycoTM_HEK293T_OG_14_10062025.raw	Raw

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Systematic Quantification of Protein O-GlcNAcylation Reveals Common and Cell-Type-Specific Responses to N-Glycosylation Inhibition in Human Cells.

Fu Longping L Yin Kejun K Xu Xing X Wu Ronghu R

Analytical chemistry 20260519 21

Both protein O-GlcNAcylation and N-glycosylation are extremely important in human cells and regulate many cellular events. While O-GlcNAcylation is known to act as a stress sensor, its changes in human cells with N-glycosylation perturbations remain to be explored. In this study, we comprehensively and site-specifically studied common and cell-type-specific responses of protein O-GlcNAcylation under N-glycosylation inhibition in three types of human cells (HEK293T, HepG2, and Jurkat cells) by in ...[more]

PMID: 42153620

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