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http://purl.uniprot.org/citations/10490590http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10490590http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10490590http://www.w3.org/2000/01/rdf-schema#comment"The death domain-containing receptor superfamily and their respective downstream mediators control whether or not cells initiate apoptosis or activate NF-kappaB, events critical for proper immune system function. A screen for upstream activators of NF-kappaB identified a novel serine-threonine kinase capable of activating NF-kappaB and inducing apoptosis. Based upon domain organization and sequence similarity, this novel kinase, named mRIP3 (mouse receptor interacting protein 3), appears to be a new RIP family member. RIP, RIP2, and mRIP3 contain an N-terminal kinase domain that share 30 to 40% homology. In contrast to the C-terminal death domain found in RIP or the C-terminal caspase-recruiting domain found in RIP2, the C-terminal tail of mRIP3 contains neither motif and is unique. Despite this feature, overexpression of the mRIP3 C terminus is sufficient to induce apoptosis, suggesting that mRIP3 uses a novel mechanism to induce death. mRIP3 also induced NF-kappaB activity which was inhibited by overexpression of either dominant-negative NIK or dominant-negative TRAF2. In vitro kinase assays demonstrate that mRIP3 is catalytically active and has autophosphorylation site(s) in the C-terminal domain, but the mRIP3 catalytic activity is not required for mRIP3 induced apoptosis and NF-kappaB activation. Unlike RIP and RIP2, mRIP3 mRNA is expressed in a subset of adult tissues and is thus likely to be a tissue-specific regulator of apoptosis and NF-kappaB activity. While the lack of a dominant-negative mutant precludes linking mRIP3 to a known upstream regulator, characterizing the expression pattern and the in vitro functions of mRIP3 provides insight into the mechanism(s) by which cells modulate the balance between survival and death in a cell-type-specific manner."xsd:string
http://purl.uniprot.org/citations/10490590http://purl.org/dc/terms/identifier"doi:10.1128/mcb.19.10.6500"xsd:string
http://purl.uniprot.org/citations/10490590http://purl.org/dc/terms/identifier"doi:10.1128/mcb.19.10.6500"xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/author"Harrington M.A."xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/author"Harrington M.A."xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/author"Goebl M.G."xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/author"Goebl M.G."xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/author"Donner D.B."xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/author"Donner D.B."xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/author"Pazdernik N.J."xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/author"Pazdernik N.J."xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/pages"6500-6508"xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/pages"6500-6508"xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/title"Mouse receptor interacting protein 3 does not contain a caspase-recruiting or a death domain but induces apoptosis and activates NF-kappaB."xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/title"Mouse receptor interacting protein 3 does not contain a caspase-recruiting or a death domain but induces apoptosis and activates NF-kappaB."xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/10490590http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/10490590http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10490590
http://purl.uniprot.org/citations/10490590http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10490590
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