Dynamic Interplay between O-Glycosylation and O-Phosphorylation of Nucleocytoplasmic Proteins: A New Paradigm for Metabolic Control of Signal Transduction and Transcription

Kazuo Kamemura, Gerald Warren Hart

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

The glycosylation of serine and threonine residues with β-O-linked N-acetylglucosamine (O-GlcNAc) is an abundant posttranslational modification of nuclear and cytoplasmic proteins in multicellular eukaryotes. This highly dynamic glycosylation{plus 45 degree rule}deglycosylation of protein is catalyzed by the nucleocytoplasmic enzymes, UDP-GlcNAc: polypeptide O-β-N-acetylglucosaminyltransferase (OGT){plus 45 degree rule}O-β-N-acetylglucosaminidase. OGT is required for embryonic stem cell viability and mouse ontogeny, thus O-GlcNAc is essential for the life of eukaryotes. The gene encoding O-GlcNAcase maps to a locus important to late-onset Alzheimer's disease. All known O-GlcNAc-modified proteins are also phosphoproteins that form reversible multimeric protein complexes. There is both a global and often site-specific reciprocal relationship between O-GlcNAc and O-phosphate in many cellular responses to stimuli. Thus, regulation of the protein-protein interaction(s) and{plus 45 degree rule}or protein function by dynamic glycosylation{plus 45 degree rule}phosphorylation has been hypothesized. In this chapter, we will review the current status of dynamic glycosylation{plus 45 degree rule}phosphorylation of several important regulatory proteins including c-Myc, estrogen receptors, Sp1, endothelial nitric oxide synthase, and β-catenin. Various aspects of subcellular localization, association with binding partners, activity, and{plus 45 degree rule}or turnover of these proteins appear to be regulated by dynamic glycosylation{plus 45 degree rule}phosphorylation in response to cellular signals or stages.

Original languageEnglish (US)
Title of host publicationProgress in Nucleic Acid Research and Molecular Biology
Pages107-136
Number of pages30
Volume73
DOIs
StatePublished - 2003

Publication series

NameProgress in Nucleic Acid Research and Molecular Biology
Volume73
ISSN (Print)00796603

Fingerprint

Staphylococcal Protein A
Glycosylation
Signal Transduction
Phosphorylation
Proteins
Eukaryota
Proto-Oncogene Proteins c-myc
Catenins
Acetylglucosaminidase
Uridine Diphosphate
Acetylglucosamine
Nitric Oxide Synthase Type III
Phosphoproteins
Threonine
Post Translational Protein Processing
Embryonic Stem Cells
Nuclear Proteins
Estrogen Receptors
Serine
Cell Survival

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Kamemura, K., & Hart, G. W. (2003). Dynamic Interplay between O-Glycosylation and O-Phosphorylation of Nucleocytoplasmic Proteins: A New Paradigm for Metabolic Control of Signal Transduction and Transcription. In Progress in Nucleic Acid Research and Molecular Biology (Vol. 73, pp. 107-136). (Progress in Nucleic Acid Research and Molecular Biology; Vol. 73). https://doi.org/10.1016/S0079-6603(03)01004-3

Dynamic Interplay between O-Glycosylation and O-Phosphorylation of Nucleocytoplasmic Proteins : A New Paradigm for Metabolic Control of Signal Transduction and Transcription. / Kamemura, Kazuo; Hart, Gerald Warren.

Progress in Nucleic Acid Research and Molecular Biology. Vol. 73 2003. p. 107-136 (Progress in Nucleic Acid Research and Molecular Biology; Vol. 73).

Research output: Chapter in Book/Report/Conference proceedingChapter

Kamemura, K & Hart, GW 2003, Dynamic Interplay between O-Glycosylation and O-Phosphorylation of Nucleocytoplasmic Proteins: A New Paradigm for Metabolic Control of Signal Transduction and Transcription. in Progress in Nucleic Acid Research and Molecular Biology. vol. 73, Progress in Nucleic Acid Research and Molecular Biology, vol. 73, pp. 107-136. https://doi.org/10.1016/S0079-6603(03)01004-3
Kamemura K, Hart GW. Dynamic Interplay between O-Glycosylation and O-Phosphorylation of Nucleocytoplasmic Proteins: A New Paradigm for Metabolic Control of Signal Transduction and Transcription. In Progress in Nucleic Acid Research and Molecular Biology. Vol. 73. 2003. p. 107-136. (Progress in Nucleic Acid Research and Molecular Biology). https://doi.org/10.1016/S0079-6603(03)01004-3
Kamemura, Kazuo ; Hart, Gerald Warren. / Dynamic Interplay between O-Glycosylation and O-Phosphorylation of Nucleocytoplasmic Proteins : A New Paradigm for Metabolic Control of Signal Transduction and Transcription. Progress in Nucleic Acid Research and Molecular Biology. Vol. 73 2003. pp. 107-136 (Progress in Nucleic Acid Research and Molecular Biology).
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