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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2009-5-19
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pubmed:abstractText |
The oncogene E2a-Pbx1 is formed by the t(1;19) translocation, which joins the N-terminal transactivation domain of E2a with the C-terminal homeodomain of PBX1. The goal of this work was to elucidate the mechanisms by which E2a-Pbx1 can lead to deregulated target gene expression. For reporter constructs it was shown that E2a-Pbx1 can activate transcription through homodimer elements (TGATTGAT) or through heterodimer elements with Hox proteins (e.g. TGATTAAT). We show a novel mechanism by which E2a-Pbx1 activates transcription of EF-9 using a promoter in intron 1 of the EF-9 gene, resulting in an aminoterminal truncated transcript. Our results indicate that the LDFS motif of E2a is essential for the transactivation of EF-9, but dispensable for transactivation of fibroblast growth factor 15. The E2a LDFS motif was also essential for proliferation of NIH3T3 fibroblasts but was dispensable for the E2a-Pbx1-induced differentiation arrest of myeloid progenitors.
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pubmed:commentsCorrections |
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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/Basic Helix-Loop-Helix...,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/E2A-Pbx1 fusion protein,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/KAT2A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins, Fusion,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TCF3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/pbx1 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1029-2403
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pubmed:author |
pubmed-author:DornAnnetteA,
pubmed-author:DuchniewiczMarlenaM,
pubmed-author:GantertMelanieM,
pubmed-author:KampsMark PMP,
pubmed-author:KolanczykMateuszM,
pubmed-author:MöbestDietrich C CDC,
pubmed-author:RäppleDanielD,
pubmed-author:ScheeleJürgen SJS,
pubmed-author:SykesDavid BDB,
pubmed-author:SykesDavid PDP,
pubmed-author:ZemojtelTomaszT
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pubmed:issnType |
Electronic
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pubmed:volume |
50
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
816-28
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pubmed:dateRevised |
2009-11-9
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pubmed:meshHeading |
pubmed-meshheading:19399691-Amino Acid Motifs,
pubmed-meshheading:19399691-Animals,
pubmed-meshheading:19399691-Base Sequence,
pubmed-meshheading:19399691-Basic Helix-Loop-Helix Transcription Factors,
pubmed-meshheading:19399691-Cell Differentiation,
pubmed-meshheading:19399691-Cell Line, Tumor,
pubmed-meshheading:19399691-Cell Proliferation,
pubmed-meshheading:19399691-DNA-Binding Proteins,
pubmed-meshheading:19399691-Fibroblasts,
pubmed-meshheading:19399691-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:19399691-Histone Acetyltransferases,
pubmed-meshheading:19399691-Homeodomain Proteins,
pubmed-meshheading:19399691-Humans,
pubmed-meshheading:19399691-Mice,
pubmed-meshheading:19399691-Molecular Sequence Data,
pubmed-meshheading:19399691-Myeloid Cells,
pubmed-meshheading:19399691-NIH 3T3 Cells,
pubmed-meshheading:19399691-Oncogene Proteins, Fusion,
pubmed-meshheading:19399691-Peptide Elongation Factor 2,
pubmed-meshheading:19399691-Proto-Oncogene Proteins,
pubmed-meshheading:19399691-Transcriptional Activation
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pubmed:year |
2009
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pubmed:articleTitle |
The Spt-Ada-Gcn5-acetyltransferase complex interaction motif of E2a is essential for a subset of transcriptional and oncogenic properties of E2a-Pbx1.
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pubmed:affiliation |
Department of Medicine I and Pharmacology I, University Hospital Freiburg, Freiburg, Germany. juergen.scheele@uniklinik-freiburg.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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