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http://purl.uniprot.org/citations/24632605http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24632605http://www.w3.org/2000/01/rdf-schema#comment"Extracellular proteins are vital for cell activities, such as cell migration. Calumenin is highly conserved among eukaryotes, but its functions are largely unclear. Here, we identify extracellular calumenin as a suppressor of cell migration and tumor metastasis. Calumenin binds to and stabilizes fibulin-1, leading to inactivation of extracellular signal-regulated kinases 1 and 2 (ERK1/2) signaling. We further identify the minimal functional domain of calumenin (amino acids 74-138 and 214-280). Depletion of calumenin induces fibulin-1- and phospho-ERK1/2 (pERK1/2)-dependent promotion of cell migration. Consistently, in hepatocellular and pancreatic carcinoma, both calumenin and fibulin-1 are downregulated. Furthermore, we show that matrix metalloproteinase-13 (MMP-13) proteolyzes fibulin-1 and that calumenin protects fibulin-1 from cleavage by MMP-13. Calumenin, together with fibulin-1, also interacts with fibronectin and depends on both syndecan-4 and α5β1-integrin to suppress ERK1/2 signaling and inhibit cell migration. Thus, extracellular calumenin regulates fibulin-1 to have crucial roles in ERK1/2 signaling and cell migration."xsd:string
http://purl.uniprot.org/citations/24632605http://purl.org/dc/terms/identifier"doi:10.1038/onc.2014.52"xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/author"Chen J."xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/author"Chen L."xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/author"Feng H."xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/author"Liu X."xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/author"Liu L."xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/author"Hao Q."xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/author"Shen B."xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/author"Wang Q."xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/author"Zheng P."xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/author"Xu S."xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/author"Teng J."xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/name"Oncogene"xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/pages"1006-1018"xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/title"Extracellular calumenin suppresses ERK1/2 signaling and cell migration by protecting fibulin-1 from MMP-13-mediated proteolysis."xsd:string
http://purl.uniprot.org/citations/24632605http://purl.uniprot.org/core/volume"34"xsd:string
http://purl.uniprot.org/citations/24632605http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24632605
http://purl.uniprot.org/citations/24632605http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24632605
http://purl.uniprot.org/uniprot/#_B2CQD6-mappedCitation-24632605http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24632605
http://purl.uniprot.org/uniprot/#_O35887-mappedCitation-24632605http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24632605
http://purl.uniprot.org/uniprot/#_Q3UG11-mappedCitation-24632605http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24632605
http://purl.uniprot.org/uniprot/#_Q08879-mappedCitation-24632605http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24632605