Role of histone H2A ubiquitination in Polycomb silencing

By Hengbin Wang, Liangjun Wang, H. Erdjument‐Bromage, M. Vidal, Paul Tempst, Richard S. Jones, Yi Zhang. Nature, 2004

1,830 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/4e21244534d507b434289745fe392d45c4dde958

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In Molecular Biology

Citations in the corpus

Histone ubiquitination: triggering gene activity. (2008, background): “associated with transcriptional silencing (Cao et al., 2005; Wang et al., 2004; Zhou et al., 2008).”
RING domain E3 ubiquitin ligases. (2009, background): “Conversely, in some cases, autoubiquitination has the opposite effect and switches on ubiquitin ligase activity, as has been reported for Bard1-Brca1 (152) and Bmi1-Ring1b (153), although the underlying mechanism remains unknown.”
Variant PRC1 Complex-Dependent H2A Ubiquitylation Drives PRC2 Recruitment and Polycomb Domain Formation (2014, background): “The co-occupancy of polycomb group proteins at target sites has largely been viewed in the context of a hierarchical recruitment model (Cao et al., 2002; Wang et al., 2004b).”
A Proteome-wide, Quantitative Survey of In Vivo Ubiquitylation Sites Reveals Widespread Regulatory Roles (2011, background): “that is known to have important biological functions (43, 44).”
Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms (2008, background): “Given this, PRC1 was proposed to act downstream of PRC2 (Wang et al., 2004b).”
Histone variants — ancient wrap artists of the epigenome (2010, positive): “Z (H2Av) are similarly necessary for repression at Polycomb-regulated genes 79,129 .”
RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA damage signaling. (2012, background): “These are targeted by the Polycomb PRC1 complex, where the Ring1B/ Bmi1 dimer is the main E3 ligase (Wang et al., 2004).”
Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. (2005, methodology): “Accumulating evidence supports a sequential model (Wang et al., 2004b) in which ESC-E(Z)-mediated H3-K27 methylation serves as a binding site for the recruitment of the PRC1 complex through the speciﬁc recognition of the H3-K27 methyl mark by the chromo domain of the Poly-comb (Pc) protein (Fischle…”
The ubiquitin code. (2012, background): “Ubiquitin Chain Assembly by RING Domain and U-Box Ligase Enzymes The enzymes that catalyze chain formation face a different speciﬁcity issue: They need to modify speciﬁc lysine residues of ubiquitin domain, this linkage speciﬁcity is likely determined by the E2 (3).”
Ring1-mediated ubiquitination of H2A restrains poised RNA polymerase II at bivalent genes in mouse ES cells (2007, positive): “Ring1B, a component of PRC1 that catalyses mono-ubiquitination of histone H2A at lysine 119 (H2Aub1”