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http://purl.uniprot.org/citations/15169888http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15169888http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15169888http://www.w3.org/2000/01/rdf-schema#comment"NF-kappa B1 p105 forms a high-affinity, stoichiometric interaction with TPL-2, a MEK kinase essential for TLR4 activation of the ERK mitogen-activated protein kinase cascade in lipopolysaccharide (LPS)-stimulated macrophages. Interaction with p105 is required to maintain TPL-2 metabolic stability and also negatively regulates TPL-2 MEK kinase activity. Here, affinity purification identified A20-binding inhibitor of NF-kappa B 2 (ABIN-2) as a novel p105-associated protein. Cotransfection experiments demonstrated that ABIN-2 could interact with TPL-2 in addition to p105 but preferentially formed a ternary complex with both proteins. Consistently, in unstimulated bone marrow-derived macrophages (BMDMs), a substantial fraction of endogenous ABIN-2 was associated with both p105 and TPL-2. Although the majority of TPL-2 in these cells was complexed with ABIN-2, the pool of TPL-2 which could activate MEK after LPS stimulation was not, and LPS activation of TPL-2 was found to correlate with its release from ABIN-2. Depletion of ABIN-2 by RNA interference dramatically reduced steady-state levels of TPL-2 protein without affecting levels of TPL-2 mRNA or p105 protein. In addition, ABIN-2 increased the half-life of cotransfected TPL-2. Thus, optimal TPL-2 stability in vivo requires interaction with ABIN-2 as well as p105. Together, these data raise the possibility that ABIN-2 functions in the TLR4 signaling pathway which regulates TPL-2 activation."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.org/dc/terms/identifier"doi:10.1128/mcb.24.12.5235-5248.2004"xsd:string
http://purl.uniprot.org/citations/15169888http://purl.org/dc/terms/identifier"doi:10.1128/mcb.24.12.5235-5248.2004"xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Howell S."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Howell S."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Soneji Y."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Soneji Y."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Janzen J."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Janzen J."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Lang V."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Lang V."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Beinke S."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Beinke S."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Ley S.C."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Ley S.C."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Symons A."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Symons A."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Watton S.J."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/author"Watton S.J."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/15169888http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string