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rdf:type |
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lifeskim:mentions |
umls-concept:C0010531,
umls-concept:C0079904,
umls-concept:C0167954,
umls-concept:C0205280,
umls-concept:C0441655,
umls-concept:C0443264,
umls-concept:C0567416,
umls-concept:C0596260,
umls-concept:C1417708,
umls-concept:C1422597,
umls-concept:C1570804,
umls-concept:C1709634,
umls-concept:C2348445
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pubmed:issue |
8
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pubmed:dateCreated |
1993-11-23
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pubmed:databankReference |
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pubmed:abstractText |
The p50 subunit of NF-kappa B is derived from the amino terminus of a 105 kilodalton precursor. The p105 carboxyl terminus, which contains ankyrin-like repeats, a feature of I kappa B molecules, regulates the cytoplasmic retention of p105 and inhibits DNA binding by the precursor. Here, we describe an I kappa B protein identical to the carboxyl-terminal region of p105. Probes spanning the COOH terminus but not the rel homology domain of p105 hybridize to a distinct 2.6-kilobase mRNA expressed in a wide range of murine tissues. The nucleotide sequence of complementary DNA clones for this transcript, in vitro translation, and immune precipitation of metabolically labeled cell lysates establish that it encodes a 70 kilodalton protein that corresponds to the COOH-terminal 607 amino acids of p105. p70 suppresses p65 and p75c-rel mediated transactivation of reporter genes under the control of NF-kappa B elements and in vitro can prevent DNA binding of p50 and p75c-rel homodimers to NF-kappa B sites. The ability of p70 to stably associate with p49 and p65 in vitro, but not inhibit DNA binding by these proteins, suggests that the specific inhibitory properties of this I kappa B may reflect its relative affinity for different rel targets. p70 phosphorylated by protein kinase A fails to inhibit DNA binding by p50 or the c-rel protein, and sequencing of radiolabeled p70 tryptic phosphopeptides establishes that protein kinase A phosphorylates serine residue 576 of p70. This finding suggests that the inhibitory activity of p70 can be regulated by signaling via the adenylate cyclase pathway.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1044-9523
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
617-27
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8398903-Amino Acid Sequence,
pubmed-meshheading:8398903-Base Sequence,
pubmed-meshheading:8398903-Cell Line,
pubmed-meshheading:8398903-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:8398903-DNA-Binding Proteins,
pubmed-meshheading:8398903-Down-Regulation,
pubmed-meshheading:8398903-Genes, Reporter,
pubmed-meshheading:8398903-Genetic Code,
pubmed-meshheading:8398903-Molecular Sequence Data,
pubmed-meshheading:8398903-Molecular Weight,
pubmed-meshheading:8398903-NF-kappa B,
pubmed-meshheading:8398903-NF-kappa B p50 Subunit,
pubmed-meshheading:8398903-Phosphorylation,
pubmed-meshheading:8398903-Protein Precursors,
pubmed-meshheading:8398903-Proto-Oncogene Proteins,
pubmed-meshheading:8398903-RNA, Messenger,
pubmed-meshheading:8398903-Sequence Homology, Amino Acid,
pubmed-meshheading:8398903-Transcription Factor RelB,
pubmed-meshheading:8398903-Transcription Factors,
pubmed-meshheading:8398903-Transcriptional Activation
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pubmed:year |
1993
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pubmed:articleTitle |
The activity of a 70 kilodalton I kappa B molecule identical to the carboxyl terminus of the p105 NF-kappa B precursor is modulated by protein kinase A.
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pubmed:affiliation |
Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital, Parkville, Victoria, Australia.
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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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