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. 2015 Feb 9;212(2):267–280. doi: 10.1084/jem.20140508

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© 2015 Liu et al.

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Figure 6. — Moesin interacts with RhoGEFs. (A) The DH/PH fragment of Vav1 was immunoprecipitated with N-moesin (aa 1–310) or C-moesin (aa 457–577). (B) Rac was pulled down with Vav1-DH/PH domain in the presence or absence of N-moesin. (C) N-moesin was immunoprecipitated with the DH/PH domain or the PDZ/RGS domain of PRG. (D) RhoA was pulled down with PRG DH/PH domain in the presence or absence of N-moesin. (E) N-moesin was immunoprecipitated with the DH/PH domain of αPIX. (F) Cdc42 was pulled down with the αPIX DH/PH domain in the presence or absence of N-moesin. (B, D, and F) *, P < 0.05 (Student’s t test). Data are representative of (blots in A–F) or are compiled from three independent experiments (graphs in B, D, and F; mean and SEM in B, D, and F).