Non-Enzymatic MGO-Glycation of SRSF2: Proteome-Wide Targets and Splicing Impact

A chemoproteomic dataset identifies 494 protein targets of methylglyoxal (MGO) glycation, a reactive metabolic byproduct linked to cancer and diabetes. The data focuses on the serine/arginine-rich splicing factor 2 (SRSF2), detailing sites where glycation destabilizes protein-RNA binding and alters RNA splicing. The dataset was authored by Yang Xiao and last updated on 2026-05-11.

Use Cases

• Identify potential protein targets of MGO-glycation based on the reported list of 494 glycated proteins.
• Analyze the functional impact of glycation on RNA binding proteins, specifically SRSF2, as described in the biophysical and experimental validation.
• Investigate mechanistic links between metabolic dysregulation (glycolysis) and disease progression (cancer, neurodegeneration) through glycation events.
• Compare MGO-mediated RNA mis-splicing effects with known oncogenic mutations like SRSF2 P95H, as suggested by the study.

Strengths

• Quantitatively profiles 494 proteome-wide glycation targets using a chemoproteomic approach.
• Provides site-specific characterization of glycation on the splicing factor SRSF2, with experimental validation of functional impact.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• The 3.3 MB file size suggests a small dataset, potentially limiting scope.

Provenance

Source

figshare

Collection Method

Quantitative chemoproteomic profiling with an alkyne-functionalized MGO probe (AlkMG), followed by biophysical modeling and RNA pulldown experiments.

Freshness

Last updated 2026-05-11 06:13:32; freshness should be verified.