Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14.

By W. Lo, R. Trievel, J. R. Rojas, Laura J. Duggan, Jer-Yuan hsu, C. D. Allis, R. Marmorstein, Shelley L. Berger. Molecules and Cells, 2000

607 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/2c73371e283721d80c80c10527e747378dddc50d

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Non-commercial Research and Educational Use including without Limitation Use in Instruction at Your Institution, Sending It to Specific Colleagues That You Know, and Providing a Copy to Your Institution's Administrator. All Other Uses, Reproduction and Distribution, including without Limitation Comm (2005, neutral): “Hopefully, a fitting procedure in which only the order parameters and the chemical shielding parameters are varied leads to a correspondence between calculated and experimental spectra close enough to recognize a sufficient number of common features.”
Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. (2001, background): “The enzymes responsible for adding and removing the phosphate group from H3-S10 were identified as the Ipl1p/ aurora-2 kinase and Glc7p/PP1 phosphatase, respectively (Hsu et al. 2000).”
Histone Recognition and Large-Scale Structural Analysis of the Human Bromodomain Family (2012, background): “The WDR9(2) interaction with H3K14ac showed strong dependence on S10 and T11 phosphorylation as well as acetylation at K18.”
Acetylation of the p53 DNA-binding domain regulates apoptosis induction. (2006, methodology): “In vitro acetylation assay—In vitro acetylation assays were performed as described previously (Lo et al., 2000).”
The Language of Histone Crosstalk (2010, background): “The first example of histone crosstalk falls into this category: the 682 Cell 142, September 3, 2010 ª2010 Elsevier Inc. phosphorylation of serine 10 on histone H3 stimulates the ability of Gcn5 to acetylate histone H3 at lysine 14 (H3K14) (Cheung et al., 2000; Lo et al., 2000) (Figure 1A).”
Essential function of histone deacetylase 1 in proliferation control and CDK inhibitor repression (2002, background): “Different modi®cations of N-terminal histone tails such as phosphorylation, methylation and acetylation have been shown to be interdependent (Cheung et al., 2000b; Clayton et al., 2000; Lo et al., 2000; Rea et al., 2000; Nakayama et al., 2001).”
Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8. (2003, methodology): “S1 nuclease protection assays were performed as described previously (Lo et al. 2000) using RNA extracted under GAL1-and SUC2-inducing conditions (2% galactose and 0.5% glucose medium , respectively).”
Deciphering the transcriptional histone acetylation code for a human gene. (2002, background): “…couplingbear bromodomains (Marmorstein and Berger, 2001), between S10 phosphorylation and K14 acetylationand the recruitment of both of these complexes to the (Cheung et al., 2000; Lo et al., 2000, 2001; Li et al., 2001;IFN- promoter is facilitated by histone acetylation Thomson et al., 2001).”