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. 2009 Jan 12;184(1):113–127. doi: 10.1083/jcb.200806044

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© 2009 Roberts-Galbraith 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 6. — Fic1 binds the SH3 domain of PCH family member Imp2. (A) Coimmunoprecipitations of Imp2-HA₃ and Fic1-FLAG₃ were performed as in Fig. 4 (B and C). IP, immunoprecipitation. (B) Fic1-TAP–containing complexes were purified from nda3-km311 imp2-HA₃ cells using IgG beads followed by TEV cleavage. These complexes were immunoprecipitated using either an anti-HA antibody or anti-Cdc15 serum, and bound proteins were detected by immunoblotting. WB, Western blot. (C) Lysates from wild-type, imp2-FLAG₃, or imp2_ΔSH3-FLAG₃ cells were incubated with recombinant bead-bound His₆ or Fic1-His₆. Bound proteins were detected by immunoblotting. (D) An in vitro binding experiment was performed with MBP-Imp2SH3 and Fic1-His₆ as in Fig. 4 E. (E) Wild-type, imp2_ΔSH3-HA₃, and imp2Δ cells were fixed and imaged as in Fig. 1 A (quantitation in Fig. S4 D, available at http://www.jcb.org/cgi/content/full/jcb.200806044/DC1). (F) Imp2_ΔSH3-GFP was visualized in live cells. BF, bright field. Bars: (E) 10 μm; (F) 5 μm.