Hyper-O-GlcNAcylation of YB-1 affects Ser102 phosphorylation and promotes cell proliferation in hepatocellular carcinoma.

摘要: As an essential post-translational modification, O-GlcNAcylation has been thought to be able modulate various nuclear and cytoplasmic proteins is emerging as a key regulator of multiple biological processes, such transcription, cell growth, signal transduction, motility. Recently, authoritative glycomics analyses have reported extensive crosstalk between phosphorylation, which always dynamically interplay with each other regulate signaling, cellular processes. Also, plentiful studies shown close correlation YB-1 phosphorylation tumorigenesis. Therefore, our study aimed determine whether was O-GlcNAc modified modification could interact its during the process HCC development. Western blot immunohistochemistry were firstly conducted reveal obvious up-regulation YB-1, OGT in tissues. What more, not only identified O-GlcNAcylated but hyper-O-GlcNAcylation demonstrated facilitate proliferation dependent manner. Moreover, we detected four specific sites confirmed T126A most effective mutant via O-GlcNAcylation-phosphorylation interaction. Even more interestingly, discovered that T126A-induced retardation subdued transcriptional activity partially reversed by T126A/S102E mutant. From all above, it difficult find glycosylated-YB-1 mainly enhanced through congenerous actions thus played indispensable roles fine-tuning procession HCC.