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. 2004 Nov 29;101(49):17126–17131. doi: 10.1073/pnas.0407492101

Fig. 1.

Fig. 1.

ERα binds directly to striatin via amino acids 183–253 of the ER. (A) Schematic representation of relevant domains of striatin. (B) Striatin coimmunoprecipitates with ERα in a variety of cells, including cells that endogenously express ERα [EAhy926 cells (human endothelial cell line), MCF7 cells (human breast cancer cell line), and GH3B6 cells (rat pituitary cell line)] and ERα-null cells transfected with an ERα expression plasmid [Rad91 cells (human radial artery-derived vascular smooth muscle cell line)]. IP, immunoprecipitation of ERα; NI, nonimmune immunoprecipitation; L, fraction of total cell lysates. (C) Short-term E2 treatment enhances complex formation between ERα and striatin. ERα was immunoprecipitated from Rad91 cells transfected with ERα, with or without exposure to 10–8 M E2 for 20 min. (D) Striatin binds ERα directly. GST fusion proteins were incubated with lysates of Rad91 cells transfected with ERα (Left) or with recombinant ERα (Right). (E) Striatin binds to amino acids 183–253 of ERα. (Upper) Schematic representation of ERα fragments used in GST pulldown experiments. (Lower) GST fusion proteins containing full-length ERα or ERα fragments were incubated with lysates of Cos1 cells.