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http://purl.uniprot.org/citations/18930133http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18930133http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18930133http://www.w3.org/2000/01/rdf-schema#comment"IKKbeta serves as a central intermediate signaling molecule in the activation of the NF-kappaB pathway. However, the precise mechanism for the termination of IKKbeta activity is still not fully understood. Using a functional genomic approach, we have identified two protein serine/threonine phosphatases, PPM1A and PPM1B, as IKKbeta phosphatases. Overexpression of PPM1A or PPM1B results in dephosphorylation of IKKbeta at Ser177 and Ser181 and termination of IKKbeta-induced NF-kappaB activation. PPM1A and PPM1B associate with the phosphorylated form of IKKbeta, and the interaction between PPM1A/PPM1B and IKKbeta is induced by TNFalpha in a transient fashion in the cells. Furthermore, knockdown of PPM1A and PPM1B expression enhances TNFalpha-induced IKKbeta phosphorylation, NF-kappaB nuclear translocation and NF-kappaB-dependent gene expression. These data suggest that PPM1A and PPM1B play an important role in the termination of TNFalpha-mediated NF-kappaB activation through dephosphorylating and inactivating IKKbeta."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.org/dc/terms/identifier"doi:10.1016/j.cellsig.2008.09.012"xsd:string
http://purl.uniprot.org/citations/18930133http://purl.org/dc/terms/identifier"doi:10.1016/j.cellsig.2008.09.012"xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Chu M."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Chu M."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Lu X."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Lu X."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Lin X."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Lin X."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Sun W."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Sun W."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Fu S."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Fu S."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Yang J."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Yang J."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Yu Y."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Yu Y."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Tan X."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Tan X."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Zhang D."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Zhang D."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Shen T."xsd:string
http://purl.uniprot.org/citations/18930133http://purl.uniprot.org/core/author"Shen T."xsd:string