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. 2010 Sep 15;21(18):3232–3246. doi: 10.1091/mbc.E09-05-0408

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© 2010 by The American Society for Cell Biology

This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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Figure 6. — Identification of a RhoA-binding motif within the BCH domain of p50RhoGAP. (A) Multiple sequence alignments of BCH domains from Homo sapiens BNIP-Sα (AY078983) and p50RhoGAP/Cdc42GAP (Q07960) using ClustalW and formatted using BOXSHADE. Identical residues are shaded black whereas similar or conserved ones are in gray. The region corresponding to the previously described Rho-binding motif in BNIP-Sα (Zhou et al., 2006) was underlined. (B) Schematic diagram of NBCH domain and its mutants. (C) Cells were cotransfected with HA-tagged RhoA and FLAG-tagged NBCH wild type or mutants as depicted in Figure 6B. Lysates were immunoprecipitated (IP) with anti-FLAG beads, and the associated proteins were separated on SDS-PAGE, blotted, and probed with HA antibody. Expression of FLAG-NBCH constructs and HA- RhoA were verified by Western blot analyses of the whole cell lysates (WCL) using anti-FLAG (third panel) and anti-HA (bottom panel), respectively. The bound RhoA was detected by anti-HA (top panel), and equal loading of IP beads were verified by anti-FLAG (second panel).