| http://purl.uniprot.org/citations/18503409 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18503409 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18503409 | http://www.w3.org/2000/01/rdf-schema#comment | "Post-translational modification by isoprenylation is a pivotal process for the correct functioning of many signalling proteins. The Drosophila melanogaster cGMP-PDE (cGMP-specific phosphodiesterase) DmPDE5/6 possesses a CaaX-box prenylation signal motif, as do several novel cGMP-PDEs from insect and echinoid species (in CaaX, C is cysteine, a is an aliphatic amino acid and X is 'any' amino acid). DmPDE5/6 is prenylated in vivo at Cys(1128) and is localized to the plasma membrane when expressed in Drosophila S2 cells. Site-directed mutagenesis of the prenylated cysteine residue (C1128S-DmPDE5/6), pharmacological inhibition of prenylation or co-expression of DmPrBP (Drosophila prenyl-binding protein)/delta each alters the subcellular localization of DmPDE5/6. Thus prenylation constitutes a critical post-translational modification of DmPDE5/6 for membrane targeting. Co-immunoprecipitation and subcellular-fractionation experiments have shown that DmPDE5/6 interacts with DmPrBP/delta in Drosophila S2 cells. Transgenic lines allow targeted expression of tagged prenylation-deficient C1128S-DmPDE5/6 in Type I (principal) cells in Drosophila Malpighian tubules, an in vivo model for DmPDE5/6 function. In contrast with wild-type DmPDE5/6, which was exclusively associated with the apical membrane, the C1128S-DmPDE5/6 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-DmPDE5/6, active transport of cGMP is affected in the same way as it is by DmPDE5/6. This suggests that, in addition to prenylation and interaction with DmPrBP/delta, further functional membrane-targeting signals exist within DmPDE5/6."xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20080560"xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20080560"xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/author | "Houslay M.D."xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/author | "Houslay M.D."xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/author | "Day J.P."xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/author | "Day J.P."xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/author | "Cleghon V."xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/author | "Cleghon V."xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/author | "Davies S.-A."xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/author | "Davies S.-A."xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/pages | "363-374"xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/pages | "363-374"xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/title | "Regulation of a Drosophila melanogaster cGMP-specific phosphodiesterase by prenylation and interaction with a prenyl-binding protein."xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/title | "Regulation of a Drosophila melanogaster cGMP-specific phosphodiesterase by prenylation and interaction with a prenyl-binding protein."xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/volume | "414"xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://purl.uniprot.org/core/volume | "414"xsd:string |
| http://purl.uniprot.org/citations/18503409 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18503409 |
| http://purl.uniprot.org/citations/18503409 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18503409 |