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. 2009 Nov 2;187(3):335–342. doi: 10.1083/jcb.200906178

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© 2009 Niault et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 1. — Raf-1 interacts with the Rok-α kinase domain. (A) Rok-α and Raf-1 proteins used in this study are shown. The phosphorylation and Ras-binding site mutants are indicated. (B and C) HA-tagged Rok-α was immunoprecipitated from COS-1 cells cotransfected with Rok-α and FL Raf-1. Input (1.5%) and the immunoprecipitates (IP) were immunoblotted with Raf-1, HA (B), or Rok-α (C) antibodies. *, unspecified band. The amount of Raf-1 coprecipitating with the Rok-α mutant proteins is plotted as fold of FL Raf-1–Rok-α interaction (set as 1; mean ± SD of four experiments). (D) Fluorescence lifetime (τ), GFP intensity, and mRFP1 intensity in MCF-7 cells transfected with the indicated constructs. RhoAV14 expression was verified by staining with Flag antibody. The cell marked with the asterisks was excluded from the cumulative FRET efficiency analysis in E because of insufficient photon counts (see Material and methods). Inset shows a magnified view of the boxed region. (E) Percentage of FRET efficiency (mean ± SD of three experiments) is shown. **, P < 0.01; ***, P < 0.005. Bars, 20 µm.

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