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O-GlcNAcylation is a reversible and dynamic post-translational modification of proteins in mammalian cells. The O-GlcNAc cycle is regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). This modification is crucial in essential cellular processes, including transcription, cell cycle regulation, stress response, and protein degradation.
Altered O-GlcNAcylation has been linked to diseases such as cancer, diabetes, and neurodegenerative disorders. Recently, many methods have been developed to identify OGT substrates and investigate their functions, but there remains a strong need for more efficient techniques.
A study showcased the effectiveness of a peptide microarray approach for discovering novel OGT substrates and examining their specificity. Notably, the protein RBL-2, a significant regulator of cell division and may act as a tumor suppressor, was identified as a substrate for three OGT isoforms. Through peptide alanine scanning, it was identified Ser 420 as a potential O-GlcNAc modification site in RBL-2. This approach will be valuable for discovering new OGT substrates and studying OGT specificity. The FAM-labeled peptide GSEIENLLERRTVLQLLLGNPNK is valuable for the study.
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