Fig. 5 | Nature Communications

Fig. 5

From: Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6

Fig. 5

Functional comparison of PrBP/δ and RhoGDI. a Schematic model of RhoGDI-induced solubilization of RhoGTPase. The cavity of apo-RhoGDI (PDB entry 1DOA)41 is in the closed conformation. Interaction of the N-terminal “regulatory arm” of RhoGDI with its binding partner on the membrane induces opening of the cavity and allows translocation of the isoprene moiety (symbolized by the red stick) of the RhoGTPase from the membrane into the cavity of RhoGDI and thereby solubilization of the RhoGTPase. b Schematic model PrBP/δ-induced solubilization of PDE6. Apo-PrBP/δ harbors a preshaped deep hydrophobic cavity but lacks an N-terminal domain that could function like the regulatory arm of RhoGDI. The doubly-prenylated PDE6 exists in equilibrium of membrane-associated and soluble species. Dissociation of membrane-associated PDE6 involves sequestering of soluble fraction of PDE6 by two copies of PrBP/δ. Depletion of soluble species of PDE6 eventually leads to complete dissociation of the membrane-associated fraction (“dissociation by depletion mechanism”; see text for details). Farnesyl- (purple color) and geranylgeranyl moieties (red color) are shown as sticks

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