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- W2912400924 abstract "Hyper-phosphorylation of RB controls its interaction with E2F and inhibits its tumor suppressor properties. However, during G1 active RB can be mono-phosphorylated on any one of 14 CDK phosphorylation sites. Here, we used quantitative proteomics to profile protein complexes formed by each mono-phosphorylated RB isoform (mP-RB) and identified the associated transcriptional outputs. The results show that the 14 sites of mono-phosphorylation co-ordinate RB's interactions and confer functional specificity. All 14 mP-RBs interact with E2F/DP proteins, but they provide different shades of E2F regulation. RB mono-phosphorylation at S811, for example, alters RB transcriptional activity by promoting its association with NuRD complexes. The greatest functional differences between mP-RBs are evident beyond the cell cycle machinery. RB mono-phosphorylation at S811 or T826 stimulates the expression of oxidative phosphorylation genes, increasing cellular oxygen consumption. These results indicate that RB activation signals are integrated in a phosphorylation code that determines the diversity of RB activity." @default.
- W2912400924 created "2019-02-21" @default.
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- W2912400924 date "2019-03-01" @default.
- W2912400924 modified "2023-10-18" @default.
- W2912400924 title "A Code of Mono-phosphorylation Modulates the Function of RB" @default.
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- W2912400924 doi "https://doi.org/10.1016/j.molcel.2019.01.004" @default.
- W2912400924 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6424368" @default.
- W2912400924 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30711375" @default.
- W2912400924 hasPublicationYear "2019" @default.
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