pubmed-article:8290251 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8290251 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
pubmed-article:8290251 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
pubmed-article:8290251 | lifeskim:mentions | umls-concept:C0056695 | lld:lifeskim |
pubmed-article:8290251 | lifeskim:mentions | umls-concept:C1148798 | lld:lifeskim |
pubmed-article:8290251 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:8290251 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
pubmed-article:8290251 | lifeskim:mentions | umls-concept:C1517317 | lld:lifeskim |
pubmed-article:8290251 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:8290251 | pubmed:dateCreated | 1994-2-24 | lld:pubmed |
pubmed-article:8290251 | pubmed:abstractText | Three related clones encoding proteins (ATFa1, 2 and 3) with specific ATF/CRE DNA-binding activities have been isolated from HeLa cell cDNA libraries. All three isoforms have weak effects on the basal activity of the adenovirus E2a promoter. We present evidence suggesting that a C-terminal element of the ATFa molecules negatively interferes with the intrinsic activation function of these proteins. We also show that coexpression of ATFa with c-Jun, Jun-B or Jun-D stimulates ATFa-dependent reporter activity, while coexpression of c-Fos has no effect. Deletion analyses indicate that the metal-binding region of ATFa is dispensible for this effect, but that the domain comprising the leucine-zipper region of ATFa is required. Reciprocal co-immunoprecipitation experiments and electrophoretic band-shift assays with in vitro synthesized proteins reveal direct interactions between ATFa and Jun or Fos. The ATFa/c-Jun heterodimers, but not the ATFa/c-Fos complexes, bind efficiently to ATF, CRE or AP1 sites. The detection of ATFa-Jun complexes in crude extracts from HeLa cells transfected with ATFa and c-Jun expression vectors suggests that such ATFa/c-Jun heterodimers also form in vivo. Altogether these results indicate that the ATFa proteins may contribute to the modulation of the activity of the Jun/Fos complexes by altering their DNA-binding and transcriptional properties. | lld:pubmed |
pubmed-article:8290251 | pubmed:language | eng | lld:pubmed |
pubmed-article:8290251 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8290251 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8290251 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8290251 | pubmed:month | Feb | lld:pubmed |
pubmed-article:8290251 | pubmed:issn | 0950-9232 | lld:pubmed |
pubmed-article:8290251 | pubmed:author | pubmed-author:KedingerCC | lld:pubmed |
pubmed-article:8290251 | pubmed:author | pubmed-author:LutzYY | lld:pubmed |
pubmed-article:8290251 | pubmed:author | pubmed-author:GoetzJJ | lld:pubmed |
pubmed-article:8290251 | pubmed:author | pubmed-author:BoccoJ LJL | lld:pubmed |
pubmed-article:8290251 | pubmed:author | pubmed-author:ChattonBB | lld:pubmed |
pubmed-article:8290251 | pubmed:author | pubmed-author:GaireMM | lld:pubmed |
pubmed-article:8290251 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8290251 | pubmed:volume | 9 | lld:pubmed |
pubmed-article:8290251 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8290251 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8290251 | pubmed:pagination | 375-85 | lld:pubmed |
pubmed-article:8290251 | pubmed:dateRevised | 2010-2-4 | lld:pubmed |
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pubmed-article:8290251 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:8290251 | pubmed:articleTitle | Jun and Fos heterodimerize with ATFa, a member of the ATF/CREB family and modulate its transcriptional activity. | lld:pubmed |
pubmed-article:8290251 | pubmed:affiliation | Laboratoire de Génétique Moléculaire des Eucaryotes (CNRS), Unité 184 (INSERM), Institut de Chimie Biologique, Strasbourg, France. | lld:pubmed |
pubmed-article:8290251 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8290251 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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