O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability
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چکیده
منابع مشابه
O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability.
The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown. O-GlcNAc transferase utilizes UDP-GlcNAc, the end product of hexosamine biosynthesis, to catalyze this modification. The availability of UDP-GlcNAc correlates with glycosylation l...
متن کاملInsulin stimulates and diabetes inhibits O-linked N-acetylglucosamine transferase and O-glycosylation of Sp1.
Insulin stimulates both the biosynthesis of transcription factor Sp1 and its O-linked N-acetylglucosaminylation (O-GlcNAcylation), which promotes nuclear localization of Sp1 and its ability to transactivate calmodulin (CaM) gene transcription. To investigate this further, we incubated H-411E liver cells with insulin (10,000 microU/ml) and quantified the subcellular distribution of O-GlcNAc tran...
متن کاملCardioprotection by N-acetylglucosamine linkage to cellular proteins.
BACKGROUND The modification of proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) represents a key posttranslational modification that modulates cellular function. Previous data suggest that O-GlcNAc may act as an intracellular metabolic or stress sensor, linking glucose metabolism to cellular function. Considering this, we hypothesized that augmentation of O-GlcNAc levels represents an...
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From the ‡Department of Biochemistry, Nagoya University School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya 466-8550, Japan, Thios Biotechnology, Oakland, California 94609, the **Department of MicrobiologyImmunology, Northwestern University School of Medicine, Chicago, Illinois 60611-3008, and the §§Program of Molecular Pathology, Aichi Cancer Center, Research Institute, 1-1 Kanokoden, Chikus...
متن کاملGlycan-dependent signaling: O-linked N-acetylglucosamine.
The addition of O-linked N-acetylglucosamine (O-GlcNAc) to target proteins may serve as a signaling modification analogous to protein phosphorylation. Like phosphorylation, O-GlcNAc is a dynamic modification occurring in the nucleus and cytoplasm. Various analytical methods have been developed to detect O-GlcNAc and distinguish it from glycosylation in the endomembrane system. Many target molec...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2001
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.111099998