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rdf:type |
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lifeskim:mentions |
umls-concept:C0007586,
umls-concept:C0007590,
umls-concept:C0007634,
umls-concept:C0208973,
umls-concept:C0243125,
umls-concept:C0699900,
umls-concept:C0851285,
umls-concept:C1517892,
umls-concept:C1519877,
umls-concept:C1567709,
umls-concept:C1704666,
umls-concept:C1710082,
umls-concept:C2698932
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pubmed:issue |
6
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pubmed:dateCreated |
1997-1-30
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pubmed:abstractText |
The proteins RAG-1 and RAG-2 are essential for initiation of V(D)J recombination. In dividing cells, RAG-2 accumulates during G1 and is undetectable during the S and G2/M cell cycle phases. A conserved degradation signal, including an essential CDK phosphorylation site at Thr-490, regulates RAG-2 accumulation during cell division and links V(D)J recombination to the cell cycle. Mutations within this signal abolish periodic degradation of RAG-2 protein in dividing cells. In mice expressing endogenous or wild-type transgenic RAG-2, V(D)J recombination intermediates accumulate preferentially in G0/G1 thymocytes; this restriction is relieved by mutation of Thr-490 to alanine (T490A). Thus, periodic destruction of RAG-2 protein couples V(D)J recombination to cell cycle phase. Using transgenic mice expressing the T490A RAG-2 mutant and a functional T cell receptor beta chain, we demonstrate that coupling of V(D)J recombination to the cell cycle is not essential for enforcement of allelic exclusion.
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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/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Joining Region,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Variable Region,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
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, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/V(D)J recombination activating...
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1074-7613
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
575-89
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8986717-Amino Acid Sequence,
pubmed-meshheading:8986717-Animals,
pubmed-meshheading:8986717-Cell Cycle,
pubmed-meshheading:8986717-Cyclin-Dependent Kinases,
pubmed-meshheading:8986717-DNA-Binding Proteins,
pubmed-meshheading:8986717-Female,
pubmed-meshheading:8986717-Genes, Immunoglobulin,
pubmed-meshheading:8986717-Half-Life,
pubmed-meshheading:8986717-Humans,
pubmed-meshheading:8986717-Immunoglobulin Fragments,
pubmed-meshheading:8986717-Immunoglobulin Joining Region,
pubmed-meshheading:8986717-Immunoglobulin Variable Region,
pubmed-meshheading:8986717-Mice,
pubmed-meshheading:8986717-Mice, Transgenic,
pubmed-meshheading:8986717-Molecular Sequence Data,
pubmed-meshheading:8986717-Mutation,
pubmed-meshheading:8986717-Nuclear Proteins,
pubmed-meshheading:8986717-Peptides,
pubmed-meshheading:8986717-Periodicity,
pubmed-meshheading:8986717-Phosphorylation,
pubmed-meshheading:8986717-Proteins,
pubmed-meshheading:8986717-Receptors, Antigen, T-Cell,
pubmed-meshheading:8986717-Recombination, Genetic,
pubmed-meshheading:8986717-Structure-Activity Relationship,
pubmed-meshheading:8986717-Thymus Gland
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pubmed:year |
1996
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pubmed:articleTitle |
A conserved degradation signal regulates RAG-2 accumulation during cell division and links V(D)J recombination to the cell cycle.
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pubmed:affiliation |
Department of Molecular Biology and Genetics, John Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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