Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation.

By Peter Cheung, K. G. Tanner, Wang L. Cheung, Paolo Sassone-Corsi, J. Denu, C. D. Allis. Molecules and Cells, 2000

825 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/ca202f7db70b7414d7dfabc566661217ecceb854

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Citations in the corpus

G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. (2002, methodology): “In addition, S10 phosphorylation facilitates the acetylation of Lys 14 in H3 (H3-K14) by the histone acetyltransferase GCN5 (Cheung et al. 2000).”
Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation. (2004, background): “Perhaps the de novo phosphorylation that is observed at sites of active transcription might affect histone H3.3 rather than histone H3, whereas the Ser 10 phosphorylation leading to chromosome condensation is specific for histone H3. This could account for the multiple observations of histone H3 ace”
Orchestrated response: a symphony of transcription factors for gene control. (2000, background): “Additonally, phosphorylation of histone H3 tails increase its recognition as a substrate for the GCN5 acetylase while both modifications are correlated with increased transcription in yeast and mammalian cells (Cheung et al. 2000; Lo et al. 2000).”
The NAD+-Dependent Deacetylase SIRT1 Modulates CLOCK-Mediated Chromatin Remodeling and Circadian Control (2008, neutral): “Interestingly, H3 Lys14 acetylation was shown to be significantly modulated by the phosphorylation of the nearby Ser10 residue ( Cheung et al., 2000b; Lo et al., 2000).”
Histone and chromatin cross-talk. (2003, background): “In mammalian cells, this mark not only inhibits methylation on K9 [27], but also precedes and promotes acetylation on K14 following specific signals ([16]; see also [8] and references therein).”
NF-κB RelA Phosphorylation Regulates RelA Acetylation (2005, background): “For example, phosphorylation of serine 10 in the tail of histone H3 increases acetylation at lysine 14 (7, 20, 21).”
An epigenetic road map for histone lysine methylation (2003, background): “Phospho- rylation (Cheung et al., 2000a) instead is a marker for activation of immediate early genes and a signal for mitotic chromatin condensation.”
Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. (2001, background): “H3-S10 phosphorylation facilitates GCN5-mediated acetylation of H3-K14 (Cheung et al. 2000; Lo et al. 2000).”
Essential function of histone deacetylase 1 in proliferation control and CDK inhibitor repression (2002, methodology): “Phosphoacetylation of histone H3 was shown to play an important role for transcriptional activation (Cheung et al., 2000a; Clayton 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).”
Mitotic Phosphorylation of Histone H3: Spatio-Temporal Regulation by Mammalian Aurora Kinases (2002, background): “target of a number of signaling kinases (8, 35, 46, 57).”