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J. Biol. Chem., Vol. 276, Issue 45, 41717-41724, November 9, 2001
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From the Tumor suppressor p53 has been shown to
transactivate epidermal growth factor receptor (EGFR) expression
through binding to a putative p53 responsive element in the EGFR
promoter between nucleotides Laboratory of Molecular Biology, CCR, NCI,
National Institutes of Health, Bethesda, Maryland 20892-4255 and the
§ Department of Immunology, Tokai University School of
Medicine, Boseidai, Isehara, Kanagawa 259-1193, Japan
265 and 239 (EGFRp53RE). Isotypes of
p63 gene products, recently identified as p53 relatives, have a similar
function to transactivate several p53 target gene promoters. However,
our results indicate that TAp63
has a very low ability to bind to the EGFRp53RE and surprisingly represses both basal EGFR promoter activity and endogenous EGFR expression. Transient transfection assays
show that the EGFR promoter region between 348 and 293, containing
two Sp1 sites, is crucial for the repression of the EGFR expression by
TAp63. Mutations in these Sp1 sites in the reporter constructs
result in loss of the TAp63 repression effect. We further show that
TAp63 directly interacts with Sp1 by immunoprecipitation analysis
and that TAp63 impairs Sp1 binding to the target DNA site in
electrophoretic mobility shift assays. These results suggest that
TAp63 is involved in the regulation of the EGFR gene expression through interactions with basal transcription factors.
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