rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5110
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pubmed:dateCreated |
1993-6-15
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pubmed:abstractText |
Antigen receptor genes are assembled by site-specific DNA rearrangement. The recombination activator genes RAG-1 and RAG-2 are essential for this process, termed V(D)J rearrangement. The activity and stability of the RAG-2 protein have now been shown to be regulated by phosphorylation. In fibroblasts RAG-2 was phosphorylated predominantly at two serine residues, one of which affected RAG-2 activity in vivo. The threonine at residue 490 was phosphorylated by p34cdc2 kinase in vitro; phosphorylation at this site in vivo was associated with rapid degradation of RAG-2. Instability was transferred to chimeric proteins by a 90-residue portion of RAG-2. Mutation of the p34cdc2 phosphorylation site of the tumor suppressor protein p53 conferred a similar phenotype, suggesting that this association between phosphorylation and degradation is a general mechanism.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/CDC2 Protein Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RAG2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Rag2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53,
http://linkedlifedata.com/resource/pubmed/chemical/V(D)J recombination activating...
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
260
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pubmed:geneSymbol |
RAG-2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
953-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8493533-3T3 Cells,
pubmed-meshheading:8493533-Amino Acid Sequence,
pubmed-meshheading:8493533-Animals,
pubmed-meshheading:8493533-CDC2 Protein Kinase,
pubmed-meshheading:8493533-Cell Line,
pubmed-meshheading:8493533-DNA-Binding Proteins,
pubmed-meshheading:8493533-Gene Rearrangement,
pubmed-meshheading:8493533-Humans,
pubmed-meshheading:8493533-Mice,
pubmed-meshheading:8493533-Molecular Sequence Data,
pubmed-meshheading:8493533-Mutation,
pubmed-meshheading:8493533-Nuclear Proteins,
pubmed-meshheading:8493533-Phosphorylation,
pubmed-meshheading:8493533-Proteins,
pubmed-meshheading:8493533-Receptors, Antigen,
pubmed-meshheading:8493533-Recombinant Fusion Proteins,
pubmed-meshheading:8493533-Transfection,
pubmed-meshheading:8493533-Tumor Suppressor Protein p53
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pubmed:year |
1993
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pubmed:articleTitle |
Regulation of V(D)J recombination activator protein RAG-2 by phosphorylation.
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pubmed:affiliation |
Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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