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All rights reserved. http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAgrBpYKqsn3klShBXuYHdbikV71ETkhj9Aq5OSZPF6Iw#_7 http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/version 20131211 http://www.tkuhn.ch/bel2nanopub/RAgrBpYKqsn3klShBXuYHdbikV71ETkhj9Aq5OSZPF6Iw#_6 http://www.w3.org/ns/prov#value The protein-protein interaction of C/EBPalpha and ASC-2 was detected by coimmunoprecipitation during granulocyte differentiation. Subsequently, GST-pull-down assay revealed that the N-terminal transactivation domain of C/EBPalpha could interact with ASC-2. This functional interaction of ASC-2 with C/EBPalpha drove a synergistic enhancement of C/EBPalpha-dependent transactivation and overexpression of the N-terminal C/EBPalpha protein in HL-60 cells inhibited ASC-2 responsiveness for C/EBPalpha activity in granulocyte differentiation, indicating C/EBPalpha dependency of ASC-2 activity. 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