| pubmed-article:11799113 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11799113 | lifeskim:mentions | umls-concept:C0014429 | lld:lifeskim |
| pubmed-article:11799113 | lifeskim:mentions | umls-concept:C0243041 | lld:lifeskim |
| pubmed-article:11799113 | lifeskim:mentions | umls-concept:C0287990 | lld:lifeskim |
| pubmed-article:11799113 | lifeskim:mentions | umls-concept:C0728940 | lld:lifeskim |
| pubmed-article:11799113 | lifeskim:mentions | umls-concept:C0015252 | lld:lifeskim |
| pubmed-article:11799113 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:11799113 | lifeskim:mentions | umls-concept:C1705178 | lld:lifeskim |
| pubmed-article:11799113 | lifeskim:mentions | umls-concept:C1705176 | lld:lifeskim |
| pubmed-article:11799113 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:11799113 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:11799113 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:11799113 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:11799113 | pubmed:dateCreated | 2002-4-8 | lld:pubmed |
| pubmed-article:11799113 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:11799113 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11799113 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11799113 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11799113 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11799113 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11799113 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11799113 | pubmed:author | pubmed-author:JiCC | lld:pubmed |
| pubmed-article:11799113 | pubmed:author | pubmed-author:AndersonEric... | lld:pubmed |
| pubmed-article:11799113 | pubmed:author | pubmed-author:FrançoisJeanJ | lld:pubmed |
| pubmed-article:11799113 | pubmed:author | pubmed-author:MolloySean... | lld:pubmed |
| pubmed-article:11799113 | pubmed:author | pubmed-author:ShimamuraSato... | lld:pubmed |
| pubmed-article:11799113 | pubmed:author | pubmed-author:ThomasGaryG | lld:pubmed |
| pubmed-article:11799113 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11799113 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:11799113 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:11799113 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11799113 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11799113 | pubmed:pagination | 12879-90 | lld:pubmed |
| pubmed-article:11799113 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
| pubmed-article:11799113 | pubmed:meshHeading | pubmed-meshheading:11799113... | lld:pubmed |
| pubmed-article:11799113 | pubmed:meshHeading | pubmed-meshheading:11799113... | lld:pubmed |
