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• W2080317996 abstract "The Brn-3a POU domain transcription factor is able to regulate the transcription of promoters containing a Brn-3 response element via its POU domain. In addition, the POU domain of Brn-3a has been shown to functionally interact with the estrogen receptor and regulate transcription from estrogen responsive promoters. The steroid receptor coactivator, Src-1, enhances transcription with a variety of steroid receptors. Here we describe a functional interaction between Brn-3a and Src-1. In glutathione S-transferase pull-down assays Src-1 was shown to specifically interact with Brn-3 proteins. Moreover, Src-1 co-immunoprecipitated from intact cells with Brn-3a. The transactivation potential of the Brn-3a/Src-1 complex was tested on both the Brn-3 responsive SNAP-25 promoter and the estrogen responsive vitellogenin promoter, in each of two different cell lines, the neuronal ND7 cell line, and the kidney BHK21 cell line. Src-1 consistently and strongly potentiated the activation of Brn-3a on the SNAP promoter construct in both the ND7 and BHK21 cell lines. The vitellogenin promoter construct, however, was only weakly activated by the Brn-3/Src-1 complex in the ND7 cells and there was even less effect on this promoter in the BHK21 cells. These results suggest a functional role for Src-1 in enhancing Brn-3a mediated transactivation, seemingly independent of nuclear hormone receptors, thus broadening the transcriptional repertoire of both Brn-3a and Src-1." @default.
• W2080317996 created "2016-06-24" @default.
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• W2080317996 date "2002-06-01" @default.
• W2080317996 modified "2023-09-25" @default.
• W2080317996 title "Functional interaction between Brn-3a and Src-1 co-activates Brn-3a-mediated transactivation" @default.
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• W2080317996 doi "https://doi.org/10.1016/s0006-291x(02)00500-4" @default.
• W2080317996 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12051737" @default.
• W2080317996 hasPublicationYear "2002" @default.
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