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http://purl.uniprot.org/citations/28196865http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28196865http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28196865http://www.w3.org/2000/01/rdf-schema#comment"Junctional adhesion molecule C (JAM-C) is an immunoglobulin superfamily protein expressed in epithelial cells, endothelial cells, and leukocytes. JAM-C has been implicated in leukocyte transendothelial migration, angiogenesis, cell adhesion, cell polarity, spermatogenesis, and metastasis. Here, we show that JAM-C undergoes S-palmitoylation on two juxtamembrane cysteine residues, Cys-264 and Cys-265. We have identified DHHC7 as a JAM-C palmitoylating enzyme by screening all known palmitoyltransferases (DHHCs). Ectopic expression of DHHC7, but not a DHHC7 catalytic mutant, enhances JAM-C S-palmitoylation. Moreover, DHHC7 knockdown decreases the S-palmitoylation level of JAM-C. Palmitoylation of JAM-C promotes its localization to tight junctions and inhibits transwell migration of A549 lung cancer cells. These results suggest that S-palmitoylation of JAM-C can be potentially targeted to control cancer metastasis."xsd:string
http://purl.uniprot.org/citations/28196865http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m116.730523"xsd:string
http://purl.uniprot.org/citations/28196865http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m116.730523"xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/author"Cao J."xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/author"Cao J."xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/author"Lin H."xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/author"Lin H."xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/author"Aramsangtienchai P."xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/author"Aramsangtienchai P."xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/author"Spiegelman N.A."xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/author"Spiegelman N.A."xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/pages"5325-5334"xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/pages"5325-5334"xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/title"S-Palmitoylation of Junctional Adhesion Molecule C Regulates Its Tight Junction Localization and Cell Migration."xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/title"S-Palmitoylation of Junctional Adhesion Molecule C Regulates Its Tight Junction Localization and Cell Migration."xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/volume"292"xsd:string
http://purl.uniprot.org/citations/28196865http://purl.uniprot.org/core/volume"292"xsd:string
http://purl.uniprot.org/citations/28196865http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28196865
http://purl.uniprot.org/citations/28196865http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28196865