pubmed-article:9130696 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9130696 | lifeskim:mentions | umls-concept:C0205102 | lld:lifeskim |
pubmed-article:9130696 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
pubmed-article:9130696 | lifeskim:mentions | umls-concept:C0287990 | lld:lifeskim |
pubmed-article:9130696 | lifeskim:mentions | umls-concept:C1522821 | lld:lifeskim |
pubmed-article:9130696 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
pubmed-article:9130696 | lifeskim:mentions | umls-concept:C1522240 | lld:lifeskim |
pubmed-article:9130696 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:9130696 | lifeskim:mentions | umls-concept:C1709708 | lld:lifeskim |
pubmed-article:9130696 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
pubmed-article:9130696 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:9130696 | pubmed:dateCreated | 1997-5-29 | lld:pubmed |
pubmed-article:9130696 | pubmed:abstractText | Activation of furin requires autoproteolytic cleavage of its 83-amino acid propeptide at the consensus furin site, Arg-Thr-Lys-Arg107/. This RER-localized cleavage is necessary, but not sufficient, for enzyme activation. Rather, full activation of furin requires exposure to, and correct routing within, the TGN/endosomal system. Here, we identify the steps in addition to the initial propeptide cleavage necessary for activation of furin. Exposure of membrane preparations containing an inactive RER-localized soluble furin construct to either: (i) an acidic and calcium-containing environment characteristic of the TGN; or (ii) mild trypsinization at neutral pH, resulted in the activation of the endoprotease. Taken together, these results suggest that the pH drop facilitates the removal of a furin inhibitor. Consistent with these findings, following cleavage in the RER, the furin propeptide remains associated with the enzyme and functions as a potent inhibitor of the endoprotease. Co-immunoprecipitation studies coupled with analysis by mass spectrometry show that release of the propeptide at acidic pH, and hence activation of furin, requires a second cleavage within the autoinhibitory domain at a site containing a P6 arginine (-Arg70-Gly-Val-Thr-Lys-Arg75/-). The significance of this cleavage in regulating the compartment-specific activation of furin, and the relationship of the furin activation pathway to those of other serine endoproteases are discussed. | lld:pubmed |
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pubmed-article:9130696 | pubmed:language | eng | lld:pubmed |
pubmed-article:9130696 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9130696 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9130696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9130696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9130696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9130696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9130696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9130696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9130696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9130696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9130696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9130696 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9130696 | pubmed:month | Apr | lld:pubmed |
pubmed-article:9130696 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:9130696 | pubmed:author | pubmed-author:ThomasGG | lld:pubmed |
pubmed-article:9130696 | pubmed:author | pubmed-author:JeanFF | lld:pubmed |
pubmed-article:9130696 | pubmed:author | pubmed-author:AndersonE DED | lld:pubmed |
pubmed-article:9130696 | pubmed:author | pubmed-author:VanSlykeJ KJK | lld:pubmed |
pubmed-article:9130696 | pubmed:author | pubmed-author:ThulinC DCD | lld:pubmed |
pubmed-article:9130696 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9130696 | pubmed:day | 1 | lld:pubmed |
pubmed-article:9130696 | pubmed:volume | 16 | lld:pubmed |
pubmed-article:9130696 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9130696 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9130696 | pubmed:pagination | 1508-18 | lld:pubmed |
pubmed-article:9130696 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
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