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. 2002 Dec 12;99(26):16701–16706. doi: 10.1073/pnas.262671599

Fig 1.

Fig 1.

Mapping a GRIP1 corepression domain. (A) The domain structure of WT and mutant GRIP1 derivatives. The basic helix–loop–helix (bHLH)/Per-ARNT-Sim (PAS) domain, NR boxes (NR box3 is shown in black), AD1, and AD2 are diagrammed. GRIP1 derivatives act as corepressors (CoR) or dominant-negatives (DN), as indicated, with respect to GR-mediated repression of AP-1. Residues 765–1,007 (shaded) are required for corepression. U2OS.G cells were transfected with indicated amounts of WT (wt) GRIP1 or ΔAD1/ΔAD2 (B), N1007 and N765 (C), or GRIP1648–1007 (D) along with 40 ng per well each of the AP-1-Luc reporter and β-actin-LacZ plasmid. Total amounts of transfected DNA were equalized with pCDNA3. Cells were treated overnight with 25 ng/ml PMA in the absence (gray) or presence (black) of 100 nM dexamethasone, and reporter activity was measured, normalized to β-galactosidase activity, and expressed as relative luminescence units (RLU). The y axis is broken to better visualize reporter activity in the absence and presence of Dex. Fold repression in each case is shown.