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Transcriptional activation

Something new to hang your HAT on

Nature volume 387, pages 654–655 (1997)Cite this article

Someone once said, “Simplicity is making the journey… with just baggage enough”. For those interested in the complexities of gene regulation, characterizing the mechanisms by which nuclear factors engage the transcriptional apparatus in response to hormonal stimulation has seemed, at times, to be an insurmountable task. But on pages 677and of this issue, Torchia et al.1 and Heery et al.2 report the identification of a short peptide motif that mediates the assembly of nuclear receptor-co-activator complexes. This result has implications for understanding the mechanisms by which nuclear receptors ultimately interact with the transcriptional machinery in a signal-dependent manner.

The nuclear receptors are a superfamily of hormone-inducible transcription factors that regulate gene expression in response to small ligands such as steroid and thyroid hormones, retinoids and vitamin D. Organized in a modular fashion, the nuclear receptors contain discrete domains that are involved in DNA recognition, ligand binding, dimerization and transactivation3. Hormone binding stimulates nuclear-receptor activity, in part by promoting a conformational change in a helical transactivation domain that is known as AF2. This change occurs through an allosteric mechanism, and it is thought to promote interactions between AF2 and proteins in the transcriptional apparatus4,5.

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Figure 1: The CREB-binding protein (CBP) is a general mediator of signal-dependent transcription.

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  1. Section on Molecular Biology, Joslin Diabetes Center, One Joslin Place, Boston, 02215, Massachusetts, USA

    Marc Montminy

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Montminy, M. Something new to hang your HAT on. Nature 387, 654–655 (1997). https://doi.org/10.1038/42594

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