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rdf:type |
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lifeskim:mentions |
umls-concept:C0017337,
umls-concept:C0043393,
umls-concept:C0090388,
umls-concept:C0205225,
umls-concept:C0871261,
umls-concept:C1332448,
umls-concept:C1514468,
umls-concept:C1704632,
umls-concept:C1704675,
umls-concept:C1706817,
umls-concept:C2911692
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pubmed:issue |
8
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pubmed:dateCreated |
1999-9-2
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pubmed:abstractText |
The 14-3-3 proteins are small abundant cytosolic eukaryotic proteins that associate with and modulate the activity of numerous other proteins. The 14-3-3 beta isoform has been shown to bind to the product of the protooncogene cRaf-1 and to facilitate its activation by Ras. Using the yeast two-hybrid system, we have demonstrated that 14-3-3 beta and another isoform, 14-3-3 tau, bind to the product of the primary response gene BRF1 and that the interaction between each isoform and BRF1 is significantly stronger than that with cRaf-1. We further demonstrated that the charge of residue 187 in 14-3-3 beta regulates its affinity for both BRF1 and cRaf-1. The interaction of either isoform with BRF1 requires both proteins to be fully intact. When all three proteins are coexpressed in a yeast trihybrid system, BRF1 interferes significantly with the binding of 14-3-3 to full-length cRaf-1 as well as to its regulatory and kinase domains. Using quantitative reverse transcription-polymerase chain reaction, 14-3-3 beta and BRF1 were found to be coexpressed in four different human tissues, suggesting a biologic role for their interaction in the regulation of cRaf-1-mediated signal transduction processes.
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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/14-3-3 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/BRF1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/BRF1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-raf,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TATA-Binding Protein Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIIIB,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine 3-Monooxygenase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1044-5498
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
653-61
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10463061-14-3-3 Proteins,
pubmed-meshheading:10463061-Amino Acid Substitution,
pubmed-meshheading:10463061-Binding Sites,
pubmed-meshheading:10463061-Gene Expression,
pubmed-meshheading:10463061-HeLa Cells,
pubmed-meshheading:10463061-Humans,
pubmed-meshheading:10463061-Mutation,
pubmed-meshheading:10463061-Protein Binding,
pubmed-meshheading:10463061-Protein Isoforms,
pubmed-meshheading:10463061-Proteins,
pubmed-meshheading:10463061-Proto-Oncogene Proteins c-raf,
pubmed-meshheading:10463061-RNA, Messenger,
pubmed-meshheading:10463061-Recombinant Fusion Proteins,
pubmed-meshheading:10463061-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10463061-Signal Transduction,
pubmed-meshheading:10463061-Static Electricity,
pubmed-meshheading:10463061-TATA-Binding Protein Associated Factors,
pubmed-meshheading:10463061-Transcription Factor TFIIIB,
pubmed-meshheading:10463061-Transcription Factors,
pubmed-meshheading:10463061-Tyrosine 3-Monooxygenase,
pubmed-meshheading:10463061-Yeasts,
pubmed-meshheading:10463061-Zinc Fingers
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pubmed:year |
1999
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pubmed:articleTitle |
The product of the primary response gene BRF1 inhibits the interaction between 14-3-3 proteins and cRaf-1 in the yeast trihybrid system.
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pubmed:affiliation |
Department of Surgery, St. Bartholomew's and the Royal London School of Medicine and Dentistry, Queen Mary and Westfield College, England. s.a.bustin@mds.qmw.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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