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http://purl.uniprot.org/citations/14517244http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14517244http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14517244http://www.w3.org/2000/01/rdf-schema#comment"Signaling by fibroblast growth factors (FGFs) and their receptors has been previously implicated in control of cell proliferation, differentiation and migration. Here we report a novel role for signaling by the EGL-15 FGFR of Caenorhabditis elegans in controlling protein degradation in differentiated muscle. Activation of EGL-15, by means of a reduction of function mutation (clr-1) affecting an inhibitory phosphatase, triggers protein degradation in adult muscle cells using a pre-existing proteolytic system. This activation is not suppressed by mutation in either of the known genes encoding FGF ligands (egl-17 or let-756) but is well suppressed when both are mutated, indicating that either ligand is sufficient and at least one is necessary for FGFR activation. Activity of the Ras pathway through mitogen-activated protein kinase (MAPK) is required to trigger protein degradation. This is the first report that degradation of intracellular protein can be triggered by a growth factor receptor using an identified signal transduction pathway. The data raise the possibility that FGF-triggered proteolysis may be relevant to muscle remodeling or dedifferentiation."xsd:string
http://purl.uniprot.org/citations/14517244http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg472"xsd:string
http://purl.uniprot.org/citations/14517244http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg472"xsd:string
http://purl.uniprot.org/citations/14517244http://purl.uniprot.org/core/author"Jacobson L.A."xsd:string
http://purl.uniprot.org/citations/14517244http://purl.uniprot.org/core/author"Jacobson L.A."xsd:string
http://purl.uniprot.org/citations/14517244http://purl.uniprot.org/core/author"Szewczyk N.J."xsd:string
http://purl.uniprot.org/citations/14517244http://purl.uniprot.org/core/author"Szewczyk N.J."xsd:string
http://purl.uniprot.org/citations/14517244http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14517244http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14517244http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/14517244http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/14517244http://purl.uniprot.org/core/pages"5058-5067"xsd:string
http://purl.uniprot.org/citations/14517244http://purl.uniprot.org/core/pages"5058-5067"xsd:string
http://purl.uniprot.org/citations/14517244http://purl.uniprot.org/core/title"Activated EGL-15 FGF receptor promotes protein degradation in muscles of Caenorhabditis elegans."xsd:string
http://purl.uniprot.org/citations/14517244http://purl.uniprot.org/core/title"Activated EGL-15 FGF receptor promotes protein degradation in muscles of Caenorhabditis elegans."xsd:string
http://purl.uniprot.org/citations/14517244http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/14517244http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/14517244http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14517244
http://purl.uniprot.org/citations/14517244http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14517244
http://purl.uniprot.org/citations/14517244http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/14517244
http://purl.uniprot.org/citations/14517244http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/14517244
http://purl.uniprot.org/uniprot/Q10656http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/14517244
http://purl.uniprot.org/uniprot/H2KZM6http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/14517244