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• W2085196189 abstract "Ubiquitination of transcription activators has been reported to regulate transcription via both proteolytic and nonproteolytic routes, yet the function of the ubiquitin (Ub) signal in the nonproteolytic process is poorly understood. By use of the heterologous transcription activator LexA-VP16 in Saccharomyces cerevisiae, we show that monoubiquitin fusion of the activator prevents stable interactions between the activator and DNA, leading to transcription inhibition without activator degradation. We identify the AAA+ ATPase Cdc48 and its cofactors as the Ub receptor responsible for extracting the monoubiquitinated activator from DNA. Our results suggest that deubiquitination of the activator is critical for transcription activation. These findings with LexA-VP16 extend in both yeast and mammalian cells to native transcription activators Met4 and R-Smads, respectively, that are known to be oligo-ubiquitinated. The results illustrate a role for Ub and Cdc48 in transcriptional regulation and gene expression that is independent of proteolysis." @default.
• W2085196189 created "2016-06-24" @default.
• W2085196189 creator A5030231956 @default.
• W2085196189 creator A5057023276 @default.
• W2085196189 creator A5076788885 @default.
• W2085196189 date "2014-03-01" @default.
• W2085196189 modified "2023-09-27" @default.
• W2085196189 title "Ubiquitin Signals Proteolysis-Independent Stripping of Transcription Factors" @default.
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• W2085196189 doi "https://doi.org/10.1016/j.molcel.2014.02.002" @default.
• W2085196189 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4005849" @default.
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