Identificador persistente para citar o vincular este elemento: http://hdl.handle.net/10553/49985
Título: The Epithelium-specific ETS Protein EHF/ESE-3 is a Context-dependent Transcriptional Repressor Downstream of MAPK Signaling Cascades
Autores/as: Tugores, Antonio 
Le, Jennifer
Sorokina, Irina
Snijders, A. J.
Duyao, Mabel
Reddy, P. Sanjeeva
Carlée, Leone
Ronshaugen, Mathew
Mushegian, Arcady
Watanaskul, Tim
Chu, Sunny
Buckler, Alan
Emtage, Spencer
McCormick, Mary Kay
Clasificación UNESCO: 32 Ciencias médicas
Fecha de publicación: 2001
Publicación seriada: Journal of Biological Chemistry 
Resumen: Exon trapping and cDNA selection procedures were used to search for novel genes at human chromosome 11p13, a region previously associated with loss of heterozygosity in epithelial carcinomas. Using these approaches, we found the ESE-2 and ESE-3 genes, coding for ETS domain-containing transcription factors. These genes lie in close proximity to the catalase gene within a approximately 200-kilobase genomic interval. ESE-3 mRNA is widely expressed in human tissues with high epithelial content, and immunohistochemical analysis with a newly generated monoclonal antibody revealed that ESE-3 is a nuclear protein expressed exclusively in differentiated epithelial cells and that it is absent in the epithelial carcinomas tested. In transient transfections, ESE-3 behaves as a repressor of the Ras- or phorbol ester-induced transcriptional activation of a subset of promoters that contain ETS and AP-1 binding sites. ESE-3-mediated repression is sequence- and context-dependent and depends both on the presence of high affinity ESE-3 binding sites in combination with AP-1 cis-elements and the arrangement of these sites within a given promoter. We propose that ESE-3 might be an important determinant in the control of epithelial differentiation, as a modulator of the nuclear response to mitogen-activated protein kinase signaling cascades.
URI: http://hdl.handle.net/10553/49985
ISSN: 0021-9258
DOI: 10.1074/jbc.M010930200
Fuente: Journal of Biological Chemistry[ISSN 0021-9258],v. 276, p. 20397-20406
Colección:Artículos
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