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http://purl.uniprot.org/citations/12659851http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12659851http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12659851http://www.w3.org/2000/01/rdf-schema#comment"MAPK/ERK kinase kinase 2 (MEKK2) is a member of the mitogen-activated protein kinase kinase kinase (MAP3K) family of protein kinases. MAP3Ks are components of a three-tiered protein kinase pathway in which a MAP3K phosphorylates and activates a mitogen-activated protein kinase kinase (MAP2K), which in turn activates a mitogen-activated protein kinase (MAPK). We have previously identified residues within protein kinase subdomain X in the MAP3K, MEKK1, that are critical for its interaction with the MAP2K, MKK4, and MEKK1-induced MKK4 activation. We report here that kinase subdomain X also plays a critical role in MEKK2 activity. Select point mutations in subdomain X impair MEKK2 phosphorylation of the MAP2Ks, MKK7 and MEK5, abolish MEKK2-induced activation of the MAPKs, JNK1 and ERK5, and diminish MEKK2-dependent activation of an AP-1 reporter gene. Interestingly, the spectrum of mutations in subdomain X of MEKK2 that affects its activity is overlapping with but not identical to those that have effects on MEKK1. Thus, mutations in subdomain X differentially affect MEKK2 and MEKK1."xsd:string
http://purl.uniprot.org/citations/12659851http://purl.org/dc/terms/identifier"doi:10.1016/s0006-291x(03)00387-5"xsd:string
http://purl.uniprot.org/citations/12659851http://purl.org/dc/terms/identifier"doi:10.1016/s0006-291x(03)00387-5"xsd:string
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/author"Huang J."xsd:string
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/author"Huang J."xsd:string
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/author"Tu Z."xsd:string
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/author"Tu Z."xsd:string
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/author"Lee F.S."xsd:string
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/author"Lee F.S."xsd:string
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/pages"532-540"xsd:string
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/pages"532-540"xsd:string
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/title"Mutations in protein kinase subdomain X differentially affect MEKK2 and MEKK1 activity."xsd:string
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/title"Mutations in protein kinase subdomain X differentially affect MEKK2 and MEKK1 activity."xsd:string
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/volume"303"xsd:string
http://purl.uniprot.org/citations/12659851http://purl.uniprot.org/core/volume"303"xsd:string
http://purl.uniprot.org/citations/12659851http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12659851
http://purl.uniprot.org/citations/12659851http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12659851
http://purl.uniprot.org/citations/12659851http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12659851
http://purl.uniprot.org/citations/12659851http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12659851