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. Author manuscript; available in PMC: 2012 Jan 1.
Published in final edited form as: Cell Signal. 2010 Sep 17;23(1):213–221. doi: 10.1016/j.cellsig.2010.09.005

Figure 2. Gα12 mutations uncoupled from PC1 binding interact normally with other Gα12 targets.

Figure 2

For all panels, the indicated NAAIRS mutants and QLα12 were expressed in HEK293 cells and examined in pulldown experiments as described in 2.4. (A, B) Mutant O was tested for in vitro interaction with GST fusions of p115RGS (GST-p115) and protein phosphatase-5 (GST-PP5). For each pulldown condition the binding of the mutant was compared to results for QLα12 analyzed in parallel. (C.) Mutant Z and QLα12 were tested for interaction with a GST fusion of the RGS domain of axin (GST-Axin). (D.) Mutant VV and QLα12 were tested for binding to GST-Hsp90. For all panels, the band intensities were quantified using Carestream Molecular Imaging software, and the ratio of pulldown-to-load for each mutant was compared to the pulldown-to-load ratio for QLα12 tested in parallel.