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• W2141171064 abstract "Recombinant c-Jun and c-Fos were ubiquitinylated by the ubiquitin carrier enzymes E214k, E220k, or E232k in the presence of the ubiquitin-activating enzyme, E1. Addition of ubiquitin protein ligase E3 substantially enhanced the E214k-mediated ubiquitinylation of c-Jun and c-Fos. Truncated c-Jun and c-Fos mutant proteins including wbJun and wbFos were also ubiquitinylated under the same conditions, suggesting the sites of ubiquitinylation are located within the dimerization and DNA binding domains of c-Jun and c-Fos. The E3-dependent ubiquitinylation of c-Jun was inhibited upon the heterodimerization of c-Jun with c-Fos. Further addition of E220k significantly enhanced ubiquitinylation of c-Jun in the heterodimer suggesting a regulatory role of E220k. Polyubiquitinylated c-Jun, wbFos, and wbJun, but not E220k-ubiquitinylated c-Jun, were readily degraded by the ATP-dependent 26 S multicatalytic proteases. These results suggest that the temporal control of c-Jun and c-Fos may be regulated through the ubiquitinylation pathways, and the ubiquitinylation of c-Jun and c-Fos may in turn be regulated in response to the heterodimerization between them and the cooperation between E220k and E3 mediated polyubiquitinylation. Recombinant c-Jun and c-Fos were ubiquitinylated by the ubiquitin carrier enzymes E214k, E220k, or E232k in the presence of the ubiquitin-activating enzyme, E1. Addition of ubiquitin protein ligase E3 substantially enhanced the E214k-mediated ubiquitinylation of c-Jun and c-Fos. Truncated c-Jun and c-Fos mutant proteins including wbJun and wbFos were also ubiquitinylated under the same conditions, suggesting the sites of ubiquitinylation are located within the dimerization and DNA binding domains of c-Jun and c-Fos. The E3-dependent ubiquitinylation of c-Jun was inhibited upon the heterodimerization of c-Jun with c-Fos. Further addition of E220k significantly enhanced ubiquitinylation of c-Jun in the heterodimer suggesting a regulatory role of E220k. Polyubiquitinylated c-Jun, wbFos, and wbJun, but not E220k-ubiquitinylated c-Jun, were readily degraded by the ATP-dependent 26 S multicatalytic proteases. These results suggest that the temporal control of c-Jun and c-Fos may be regulated through the ubiquitinylation pathways, and the ubiquitinylation of c-Jun and c-Fos may in turn be regulated in response to the heterodimerization between them and the cooperation between E220k and E3 mediated polyubiquitinylation." @default.
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• W2141171064 date "1996-03-01" @default.
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• W2141171064 title "Ubiquitinylation of Transcription Factors c-Jun and c-Fos Using Reconstituted Ubiquitinylating Enzymes" @default.
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• W2141171064 doi "https://doi.org/10.1074/jbc.271.9.4930" @default.
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