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http://purl.uniprot.org/citations/20974804http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20974804http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20974804http://www.w3.org/2000/01/rdf-schema#comment"Rho GTPases regulate multiple signaling pathways to control a number of cellular processes during epithelial morphogenesis. To investigate the downstream pathways through which Rho regulates epithelial apical junction formation, we screened a small interfering RNA (siRNA) library targeting 28 known Rho target proteins in 16HBE human bronchial epithelial cells. This led to the identification of the serine-threonine kinase PRK2 (protein kinase C-related kinase 2, also called PKN2). Depletion of PRK2 does not block the initial formation of primordial junctions at nascent cell-cell contacts but does prevent their maturation into apical junctions. PRK2 is recruited to primordial junctions, and this localization depends on its C2-like domain. Rho binding is essential for PRK2 function and also facilitates PRK2 recruitment to junctions. Kinase-dead PRK2 acts as a dominant-negative mutant and prevents apical junction formation. We conclude that PRK2 is recruited to nascent cell-cell contacts through its C2-like and Rho-binding domains and promotes junctional maturation through a kinase-dependent pathway."xsd:string
http://purl.uniprot.org/citations/20974804http://purl.org/dc/terms/identifier"doi:10.1128/mcb.01001-10"xsd:string
http://purl.uniprot.org/citations/20974804http://purl.org/dc/terms/identifier"doi:10.1128/mcb.01001-10"xsd:string
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/author"Magalhaes A."xsd:string
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/author"Magalhaes A."xsd:string
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/author"Hall A."xsd:string
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/author"Hall A."xsd:string
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/author"Wallace S.W."xsd:string
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/author"Wallace S.W."xsd:string
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/pages"81-91"xsd:string
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/pages"81-91"xsd:string
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/title"The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells."xsd:string
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/title"The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells."xsd:string
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/volume"31"xsd:string
http://purl.uniprot.org/citations/20974804http://purl.uniprot.org/core/volume"31"xsd:string
http://purl.uniprot.org/citations/20974804http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20974804
http://purl.uniprot.org/citations/20974804http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20974804
http://purl.uniprot.org/citations/20974804http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20974804
http://purl.uniprot.org/citations/20974804http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20974804