earticle

영어

Protein S-nitrosylation and O-GlcNAcylation are important posttranslational modifications. Biological relevance between S-nitrosylation and O-GlcNAcylation remains unclear. Our goal is to identify the crosstalk between S-nitrosylation and O-GlcNAcylation during heat-shock. Ex vivo heat-shock on mouse tissues together with in vitro heat-shock on culture cells was performed and global levels of S-nitrosylation(SNO) and O-GlcNAcylation were analyzed with Biotin-switch assay and RL2 immunoblots. We found that heat-shock induces hypo-SNO in parallel with hyper-O-GlcNAcylation. Inverted induction of hypo-SNO and hyper-O-GlcNAcylation is globally progressed in a time-dependent manner. Furthermore, heat-shock ubiquitously facilitates S-denitrosylation (SdeNO) of endogenous SNO-proteins including SNO-OGT, SNO-Hsp70, SNO-Hsp90, SNO-Akt, and SNO-actin. Particularly, SdeNO of SNO-OGT leads to enhanced OGT activity. These results provide mechanistic evidence that heat shock induces SdeNO in SNO-OGT, leading to upregulation of OGT activity, resulting in hyper-O-GlcNAcylation.