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. Author manuscript; available in PMC: 2010 Jul 1.
Published in final edited form as: Cell Signal. 2009 Mar 16;21(7):1169–1179. doi: 10.1016/j.cellsig.2009.03.006

Figure 2. Effect of vesicle size, coatomer, PI4P and PIP2 on GAP-induced hydrolysis of GTP bound to Arf1.

Figure 2

[1–521]Arf GAP2-His6 was titrated into a reaction with LUVs containing either 10% PI, 7.5% PI and 2.5% PI4P (indicated +PI4P) or 7.5% PI and 2.5% PIP2 (indicated +PIP2). A. Interaction of coatomer and PI4P. Reaction contained LUVs extruded through 1.0 μm pores with PI4P where indicated and 124 nM coatomer where indicated. B. Effect of vesicle size on PI4P- and coatomer-dependent GAP activity. GAP activity was determined in reaction mixtures containing 124 nM coatomer and LUVs containing PI4P and extruded through membranes with pores of the indicated diameters. C. Effect of vesicle size on PIP2- and coatomer-dependent GAP activity. GAP activity was determined in reaction mixtures containing 124 nM coatomer and LUVs containing PIP2 and extruded through membranes with pores of the indicated diameters.