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. Author manuscript; available in PMC: 2009 Feb 13.
Published in final edited form as: Mol Cell Endocrinol. 2007 Nov 17;283(1-2):19–31. doi: 10.1016/j.mce.2007.10.014

Figure 6. Activated GR releases INHAT from GREs through physical interaction with Set/TAF-Iβ, permitting HAT-induced acetylation of histone tails and hence gene transcription, while Set-Can suppresses GR transcriptional activity by being continuously associated with GREs and preventing GR coactivator-driven acetylation.

Figure 6

A: INHAT is associated with a GRE-containing promoter at the baseline state, binding histones and protecting them from transcription factor/nuclear receptor coactivator HAT-mediated acetylation. Once ligand becomes available, activated GR induces dissociation of INHAT from histones through physical interaction with Set/TAF-Iβ, making these histones susceptible to HAT-induced acetylation.

B: Pathologic Set-Can fusion protein remains associated with GREs in the presence of glucocorticoids, suppressing GR-induced transcriptional activity by preventing HAT-induced histone acetylation.

INHAT: inhibitor of the histone acetyltransferases, HAT: histone acetyltransferase, GR: glucocorticoid receptor, GREs: glucocorticoid response elements.