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. 2022 May 16;11:e72512. doi: 10.7554/eLife.72512

Figure 4. Impact of Y537S and D538G mutation on ligand-induced estrogen receptor alpha (ERα) SUMOylation and SRC1 coactivator binding.

SUMOylation of WT (A), Y537S (B), or D538G (C) ERα in the presence of vehicle, fulvestrant, GDC0927, raloxifene, AZD9496, 4-hydroxytamoxifen (4OHT), lasofoxifene-degrader (LA-Deg), or lasofoxifene-stabilizer (LA-Stab). Data are shown as the mean ± SEM n=3–5 biological replicates. Association of WT (D), Y537S (E), and D538G (F) ERα and the receptor-interacting domain of SRC1. Data are shown as the mean ± SEM, n=3 biologic replicates.

Figure 4—source data 1. Ligand and Mutational Influences on Estrogen Receptor SUMOylation.
The SEM values for IC50s were all within 20% except for Ral with WT (21.4%) and OHT for D538G (26.2%).
Figure 4—source data 2. IC50 of SRC1 receptor interacting domain binding to WT and mutant estrogen receptor alpha.
The SEM values for IC50s were all within 50% except for D538G with AZD9496 (52%).

Figure 4.

Figure 4—figure supplement 1. Fulvestrant-induced SUMOylation WT.

Figure 4—figure supplement 1.

(A), Y537S (B), and D538G (C) estrogen receptor alpha in the presence and absence of 5 nM estradiol (E2). Data are mean of three biological replicates ± SD.