How Staffing Patterns Impact Employment Outcomes Across Diverse D/HH Consumers

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How Staffing Patterns Impact Employment Outcomes Across Diverse D/HH Consumers

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Regulation of a Drosophila melanogaster cGMP-specific phosphodiesterase by prenylation and interaction with a prenyl-binding protein

Post-translational modification by isoprenylation is a pivotal process for the correct functioning of many signalling proteins. The <i>Drosophila</i> <i>melanogaster</i> cGMP-PDE (cGMP-specific phosphodiesterase) <i>Dm</i>PDE5/6 possesses a C<i>aa</i>X-box prenylation signal motif, as do several novel cGMP-PDEs from insect and echinoid species (in C<i>aa</i>X, C is cysteine, a is an aliphatic amino acid and X is 'any' amino acid). D<i>m</i>PDE5/6 is prenylated <i>in vivo</i> at Cys(1128) and is localized to the plasma membrane when expressed in <i>Drosophila</i> S2 cells. Site-directed mutagenesis of the prenylated cysteine residue (C1128S-DmPDE5/6), pharmacological inhibition of prenylation or co-expression of D<i>m</i>PrBP (Drosophila prenyl-binding protein)/δ each alters the subcellular-localization of D<i>m</i>PDE5/6. Thus prenylation constitutes a critical post-translational modification of D<i>m</i>PDE5/6 for membrane targeting. Co-immunoprecipitation and subcellular-fractionation experiments have shown that D<i>m</i>PDE5/6 interacts with D<i>m</i>PrBP/δ in Drosophila S2 cells. Transgenic lines allow targeted expression of tagged prenylation-deficient C1128S-D<i>m</i>PDE5/6 in Type I (principal) cells in Drosophila Malpighian tubules, ail <i>in vivo</i> model for D<i>m</i>PDE5/6 function. In contrast with wild-type D<i>m</i>PDE5/6, which was exclusively associated with the apical membrane, the C1128S-D<i>m</i>PDE5/6 Mutant form was located primarily in the cytosol, although some residual association occurred at the apical membrane. Despite the profound change in intracellular localization of C1128S-D<i>m</i>PDE5/6, active transport of cGMP is affected in the same way as it is by D<i>m</i>PDE5/6. This suggests that, in addition to prenylation and interaction with D<i>m</i>PrBP/δ, further functional membrane-targeting signals exist within D<i>m</i>PDE5/

Ras plasma membrane signalling platforms

The plasma membrane is a complex, dynamic structure that provides platforms for the assembly of many signal transduction pathways. These platforms have the capacity to impose an additional level of regulation on cell signalling networks. In this review, we will consider specifically how Ras proteins interact with the plasma membrane. The focus will be on recent studies that provide novel spatial and dynamic insights into the micro-environments that different Ras proteins utilize for signal transduction. We will correlate these recent studies suggesting Ras proteins might operate within a heterogeneous plasma membrane with earlier biochemical work on Ras signal transduction