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http://purl.uniprot.org/citations/31152061http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31152061http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31152061http://www.w3.org/2000/01/rdf-schema#comment"Collagens are the main structural component of the extracellular matrix and provide biomechanical properties to connective tissues. A critical step in collagen fibril formation is the proteolytic removal of N- and C-terminal propeptides from procollagens by metalloproteinases of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) and BMP1 (bone morphogenetic protein 1)/Tolloid-like families, respectively. BMP1 also cleaves and activates the lysyl oxidase (LOX) precursor, the enzyme catalyzing the initial step in the formation of covalent collagen cross-links, an essential process for fibril stabilization. In this study, using murine skin fibroblasts and HEK293 cells, along with immunoprecipitation, LOX enzymatic activity, solid-phase binding assays, and proteomics analyses, we report that the LOX precursor is proteolytically processed by the procollagen N-proteinases ADAMTS2 and ADAMTS14 between Asp-218 and Tyr-219, 50 amino acids downstream of the BMP1 cleavage site. We noted that the LOX sequence between the BMP1- and ADAMTS-processing sites contains several conserved tyrosine residues, of which some are post-translationally modified by tyrosine O-sulfation and contribute to binding to collagen. Taken together, these findings unravel an additional level of regulation in the formation of collagen fibrils. They point to a mechanism that controls the binding of LOX to collagen and is based on differential BMP1- and ADAMTS2/14-mediated cleavage of a tyrosine-sulfated domain."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.org/dc/terms/identifier"doi:10.1074/jbc.ra119.007806"xsd:string
http://purl.uniprot.org/citations/31152061http://purl.org/dc/terms/identifier"doi:10.1074/jbc.ra119.007806"xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/author"Dupont L."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/author"Dupont L."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/author"Paradela A."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/author"Paradela A."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/author"Bekhouche M."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/author"Bekhouche M."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/author"Bravo G."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/author"Bravo G."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/author"Colige A."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/author"Colige A."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/author"Rodriguez-Pascual F."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/author"Rodriguez-Pascual F."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/author"Rosell-Garcia T."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/author"Rosell-Garcia T."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/pages"11087-11100"xsd:string
http://purl.uniprot.org/citations/31152061http://purl.uniprot.org/core/pages"11087-11100"xsd:string