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http://purl.uniprot.org/citations/17237226http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17237226http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17237226http://www.w3.org/2000/01/rdf-schema#comment"MPP7, a previously uncharacterized member of the p55 Stardust family of membrane-associated guanylate kinase (MAGUK) proteins, was found in a tripartite complex with DLG1 and LIN7A or LIN7C. MPP7 dimerizes with all three LIN7 family members (LIN7A, -B, and -C) through interaction of the single L27 domain of LIN7 with the carboxyl-terminal L27 domain of MPP7, thereby stabilizing both proteins. The dimer of MPP7 with LIN7A or LIN7C associates with DLG1 through an interaction requiring the amino-terminal L27 domain of MPP7. The amino-terminal L27 domain of MPP7 is not sufficient for interaction with DLG1 but interacts efficiently only if MPP7 is in a complex with LIN7A or -C. Thus the specificity of interaction of DLG1 with the LIN7-MPP7 complex is determined by L27 interactions with both MPP7 and LIN7. The tripartite complex forms in a ratio of 1:1:1 and localizes to epithelial adherens junctions in a manner dependent upon MPP7. Expression of MPP7 stabilizes DLG1 in an insoluble compartment. Expression of MPP7 deleted of the PDZ or Src homology 3 domain redistributes MPP7, DLG1, and LIN7 out of adherens junctions and into the soluble cytoplasmic fraction without changing the localization of E-cadherin. Thus, the stability and localization of DLG1 to cell-cell junctions are complex functions determined by the expression and association of particular Stardust family members together with particular LIN7 family members."xsd:string
http://purl.uniprot.org/citations/17237226http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m610002200"xsd:string
http://purl.uniprot.org/citations/17237226http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m610002200"xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/author"Lyons C."xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/author"Lyons C."xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/author"Brimer N."xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/author"Brimer N."xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/author"Vande Pol S.B."xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/author"Vande Pol S.B."xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/author"Bohl J."xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/author"Bohl J."xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/pages"9392-9400"xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/pages"9392-9400"xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/title"The stardust family protein MPP7 forms a tripartite complex with LIN7 and DLG1 that regulates the stability and localization of DLG1 to cell junctions."xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/title"The stardust family protein MPP7 forms a tripartite complex with LIN7 and DLG1 that regulates the stability and localization of DLG1 to cell junctions."xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/volume"282"xsd:string
http://purl.uniprot.org/citations/17237226http://purl.uniprot.org/core/volume"282"xsd:string
http://purl.uniprot.org/citations/17237226http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17237226
http://purl.uniprot.org/citations/17237226http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17237226