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- W2063513426 abstract "The transcription factor NFATp integrates multiple signal transduction pathways through coordinate binding with basic-region leucine zipper (bZIP) proteins and other transcription factors. The NFATp monomer, even in the absence of its activation domains, recruits bZIP proteins to canonical NFAT–bZIP composite DNA elements. By contrast, the NFATp dimer and its bZIP partner bind noncooperatively to the NFAT–bZIP element of the tumor necrosis factor ( TNF ) gene promoter. This observation raises the possibility that the function of the activation domains of NFATp is dimer-specific. Here, we determine the consensus DNA binding site of the NFATp dimer, describe monomer- and dimer-specific NFATp–DNA contact patterns, and demonstrate that NFATp dimerization and dimer-specific activation subdomains are required for transcriptional activation from the TNF NFAT–bZIP element. We also show that these NFATp subdomains interact with the coactivator CBP (CREB-binding protein), which is required for NFATp-dependent TNF gene transcription. Thus, the context-specific function of the activation domains of NFAT can be potentiated by DNA-directed dimerization." @default.
- W2063513426 created "2016-06-24" @default.
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- W2063513426 date "2008-12-16" @default.
- W2063513426 modified "2023-10-17" @default.
- W2063513426 title "A dimer-specific function of the transcription factor NFATp" @default.
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- W2063513426 doi "https://doi.org/10.1073/pnas.0810648105" @default.
- W2063513426 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2604938" @default.
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