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http://purl.uniprot.org/citations/14654779http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14654779http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14654779http://www.w3.org/2000/01/rdf-schema#comment"The extracellular signal-regulated kinase (ERK) pathway plays an important role during the development and activation of B lymphocytes. We have recently shown that B-Raf is a dominant ERK activator in B-cell antigen receptor signalling. We now show that B-Raf is hyperphosphorylated upon BCR engagement and undergoes a prominent electrophoretic mobility shift. This shift correlates with ERK activation and is prevented by the MEK inhibitor U0126. Syk-deficient DT40 B cells display neither dual ERK phosphorylation nor a mobility shift of B-Raf upon BCR engagement. The inducible expression of a constitutively active B-Raf in this mutant line restores dual ERK phosphorylation and the mobility shift of endogenous B-Raf, indicating that these two events are connected to each other. By site-directed mutagenesis studies, we demonstrate that the shift is due to an ERK2-mediated feedback phosphorylation of serine/threonine residues within an evolutionary conserved SPKTP motif at the C-terminus of B-Raf. Replacement of these residues by negatively charged amino acids causes a constitutive mobility shift and a reduction of PC12 cell differentiation. We discuss a model in which ERK-mediated phosphorylation of the SPKTP motif is involved in negative feedback regulation of B-Raf."xsd:string
http://purl.uniprot.org/citations/14654779http://purl.org/dc/terms/identifier"doi:10.1038/sj.onc.1207185"xsd:string
http://purl.uniprot.org/citations/14654779http://purl.org/dc/terms/identifier"doi:10.1038/sj.onc.1207185"xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/author"Brummer T."xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/author"Brummer T."xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/author"Naegele H."xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/author"Naegele H."xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/author"Reth M."xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/author"Reth M."xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/author"Misawa Y."xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/author"Misawa Y."xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/name"Oncogene"xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/name"Oncogene"xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/pages"8823-8834"xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/pages"8823-8834"xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/title"Identification of novel ERK-mediated feedback phosphorylation sites at the C-terminus of B-Raf."xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/title"Identification of novel ERK-mediated feedback phosphorylation sites at the C-terminus of B-Raf."xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/14654779http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/14654779http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14654779
http://purl.uniprot.org/citations/14654779http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14654779