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. Author manuscript; available in PMC: 2009 Nov 1.
Published in final edited form as: Cell Signal. 2008 Jul 11;20(11):1968–1977. doi: 10.1016/j.cellsig.2008.07.007

Figure 7. Effect of mutating PH domain in region of interaction with Arf GAP domain on lipid dependent binding and GAP activity. A. Binding of isolated PH domain to LUVs.

Figure 7

The binding of PH and [H405D, N406D]PH to LUVs containing the indicated concentrations of PIP2 was measured as described in Figure 6. The data are the mean ± SEM from three experiments. B. Binding of PZA to vesicles. The PIP2 dependence of [H405D, N406D]PZA and [R407D]PZA binding to large unilamellar vesicles was compared to that of PZA. C. PIP2 dependence of Arf GAP activity. GAP activity of PZA, [H405D, N406D]PZA and [R407D]PZA was determined as described in “Materials and Methods” in the presence of large unilamellar vesicles containing PIP2 at the indicated concentration in the reaction mixture.