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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1995-6-16
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pubmed:abstractText |
O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues. Although O-GlcNAc occurs on a myriad of nuclear and cytoplasmic proteins, only a few have thus far been identified. These O-GlcNAc-bearing proteins are also modified by phosphorylation and form reversible multimeric complexes. Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells. O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells. Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-1512232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-1521738,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-1583718,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-1587829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-1748630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-1865909,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-2006410,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-2105947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-2182631,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-2190987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-2233723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-2663470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-2673024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-3139301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-3299053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-3333275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-3526329,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-3571327,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-3885045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-3915537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-4063349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-7510249,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-8108117,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-8139512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-8146655,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-8193530,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-8302604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-8397370,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7753821-8486697
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
92
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4417-21
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7753821-Acetylglucosamine,
pubmed-meshheading:7753821-Amidohydrolases,
pubmed-meshheading:7753821-Animals,
pubmed-meshheading:7753821-Binding Sites,
pubmed-meshheading:7753821-CHO Cells,
pubmed-meshheading:7753821-Cattle,
pubmed-meshheading:7753821-Cell Line,
pubmed-meshheading:7753821-Chromatography, Affinity,
pubmed-meshheading:7753821-Cloning, Molecular,
pubmed-meshheading:7753821-Cricetinae,
pubmed-meshheading:7753821-Glycoside Hydrolases,
pubmed-meshheading:7753821-Glycosylation,
pubmed-meshheading:7753821-Helix-Loop-Helix Motifs,
pubmed-meshheading:7753821-Humans,
pubmed-meshheading:7753821-Leucine Zippers,
pubmed-meshheading:7753821-Macromolecular Substances,
pubmed-meshheading:7753821-Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase,
pubmed-meshheading:7753821-Protein Biosynthesis,
pubmed-meshheading:7753821-Protein Processing, Post-Translational,
pubmed-meshheading:7753821-Proto-Oncogene Proteins c-myc,
pubmed-meshheading:7753821-Rats,
pubmed-meshheading:7753821-Recombinant Proteins,
pubmed-meshheading:7753821-Sequence Deletion,
pubmed-meshheading:7753821-Serine,
pubmed-meshheading:7753821-Spodoptera,
pubmed-meshheading:7753821-Threonine,
pubmed-meshheading:7753821-Transcriptional Activation,
pubmed-meshheading:7753821-Transfection
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pubmed:year |
1995
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pubmed:articleTitle |
Glycosylation of the c-Myc transactivation domain.
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pubmed:affiliation |
Biochemistry, Cellular and Molecular Biology Training Program, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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