RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/19098003http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19098003http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19098003http://www.w3.org/2000/01/rdf-schema#comment"Cancer drugs targeting ErbB receptors, such as epidermal growth factor receptor and ErbB2, are currently in clinical use. However, the role of ErbB4 as a potential cancer drug target has remained controversial. Recently, somatic mutations altering the coding region of ErbB4 were described in patients with breast, gastric, colorectal, or non-small cell lung cancer, but the functional significance of these mutations is unknown. Here we demonstrate that 2 of 10 of the cancer-associated mutations of ErbB4 lead to loss of ErbB4 kinase activity due to disruption of functionally important structural features. Interestingly, the kinase-dead ErbB4 mutants were as efficient as wild-type ErbB4 in forming a heterodimeric neuregulin receptor with ErbB2 and promoting phosphorylation of Erk1/2 and Akt in an ErbB2 kinase-dependent manner. However, the mutant ErbB4 receptors failed to phosphorylate STAT5 and suppressed differentiation of MDA-MB-468 mammary carcinoma cells. These findings suggest that the somatic ErbB4 mutations have functional consequences and lead to selective changes in ErbB4 signaling."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m805438200"xsd:string
http://purl.uniprot.org/citations/19098003http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m805438200"xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/author"Sundvall M."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/author"Sundvall M."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/author"Johnson M.S."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/author"Johnson M.S."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/author"Hollmen M."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/author"Hollmen M."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/author"Elenius K."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/author"Elenius K."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/author"Kurppa K."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/author"Kurppa K."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/author"Repo S."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/author"Repo S."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/author"Tvorogov D."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/author"Tvorogov D."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/pages"5582-5591"xsd:string
http://purl.uniprot.org/citations/19098003http://purl.uniprot.org/core/pages"5582-5591"xsd:string