| http://purl.uniprot.org/citations/11799113 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11799113 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11799113 | http://www.w3.org/2000/01/rdf-schema#comment | "The propeptide of furin has multiple roles in guiding the activation of the endoprotease in vivo. The 83-residue N-terminal propeptide is autoproteolytically excised in the endoplasmic reticulum (ER) at the consensus furin site, -Arg(104)-Thr-Lys-Arg(107)-, but remains bound to furin as a potent autoinhibitor. Furin lacking the propeptide is ER-retained and proteolytically inactive. Co-expression with the propeptide, however, restores trans-Golgi network (TGN) localization and enzyme activity, indicating that the furin propeptide is an intramolecular chaperone. Blocking this step results in localization to the ER-Golgi intermediate compartment (ERGIC)/cis-Golgi network (CGN), suggesting the ER and ERGIC/CGN recognize distinct furin folding intermediates. Following transport to the acidified TGN/endosomal compartments, furin cleaves the bound propeptide at a second, internal P1/P6 Arg site (-Arg-Gly-Val(72)-Thr-Lys-Arg(75)-) resulting in propeptide dissociation and enzyme activation. Cleavage at Arg(75), however, is not required for proper furin trafficking. Kinetic analyses of peptide substrates indicate that the sequential pH-modulated propeptide cleavages result from the differential recognition of these sites by furin. Altering this preference by converting the internal site to a canonical P1/P4 Arg motif (Val(72) --> Arg) caused ER retention and blocked activation of furin, demonstrating that the structure of the furin propeptide mediates folding of the enzyme and directs its pH-regulated, compartment-specific activation in vivo."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m108740200"xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m108740200"xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/author | "Fei H."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/author | "Fei H."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/author | "Shimamura S."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/author | "Shimamura S."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/author | "Thomas G."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/author | "Thomas G."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/author | "Anderson E.D."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/author | "Anderson E.D."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/author | "Molloy S.S."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/author | "Molloy S.S."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/author | "Jean F."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/author | "Jean F."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/pages | "12879-12890"xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/pages | "12879-12890"xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/title | "The ordered and compartment-specfific autoproteolytic removal of the furin intramolecular chaperone is required for enzyme activation."xsd:string |
| http://purl.uniprot.org/citations/11799113 | http://purl.uniprot.org/core/title | "The ordered and compartment-specfific autoproteolytic removal of the furin intramolecular chaperone is required for enzyme activation."xsd:string |