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

Fig. 3.

Fig. 3.

Striatin assembles a complex containing ERα and Gαi. (A) E2 induces Gαi to complex with striatin and ERα, and this is blocked by coincubation with PTX or the ER antagonist ICI 182,780 (ICI). Equivalent recovery of Gαi was shown by immunoblotting (data not shown). SFM, serum-free medium. (B) PTX abolishes E2-induced phosphorylation of MAPK. *, P < 0.05 vs. SFM. n = 3 independent experiments. (C)Gαi does not bind directly to ERα. (D)Gαi binds to the C terminus of striatin. GST fusion proteins containing either full-length striatin or the N terminus of striatin (striatin1–203) were incubated with lysates of Cos1 cells transfected with Gαi. (E) Striatin is required for complex formation between ERα and Gαi. GST or GST–Gαi fusion proteins were incubated with recombinant (rER), in the absence or presence of purified full-length striatin or striatin1–203. rERα, recombinant ERα. (F) Striatin forms a complex with eNOS. eNOS was identified by immunoblotting in GST fusion pulldowns and by coimmunoprecipitation of lysates from EAhy926 cells.