Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation.

By Mariana de Napoles, J. E. Mermoud, Rika Wakao, Y-A Tang, Mitusuhiro Endoh, Ruth Appanah, T. Nesterova, Jose Silva, A. Otte, M. Vidal and 2 more. Developmental Cell, 2004

992 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/80c7134cdc81721ee5348270af473164dee863ef

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Citations in the corpus

Systematic discovery of Xist RNA binding proteins (2015, background): “We identified Rnf2 (also known as Ring2 or Ring1b), the catalytic subunit of Polycomb repressive complex 1 (PRC1) that deposits the repressive lysine119 monoubiquitination on histone H2A (H2AK119ub) over the inactive X chromosome (de Napoles et al., 2004; Fang et al., 2004).”
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).”
RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. (2007, neutral): “We exploited the recent findings showing that inhibition of the 26S proteasome causes a rapid depletion of free nuclear ubiquitin due to accumulation of nondegraded polyubiquitylated proteins in the cytosol ( Dantuma et al., 2006 ).”
How is pluripotency determined and maintained? (2007, background): “ES cells lacking Rnf2/Ring1 , a component of PRC1, are also viable and show decreased amounts of histone H2A ubiquitination (Napoles et al., 2004).”
Polycomb group proteins: multi-faceted regulators of somatic stem cells and cancer. (2010, positive): “The RING1 protein hasmonoubiquitylation E3 ligase activity specific for the lysine 119 of H2A (H2AK119ub), a mark associated with repressive chromatin structure (de Napoles et al., 2004; Wang et al., 2004).”
Ring1-mediated ubiquitination of H2A restrains poised RNA polymerase II at bivalent genes in mouse ES cells (2007, background): “Ring1B, a component of PRC1 that catalyses mono-ubiquitination of histone H2A at lysine 119 (H2Aub1”
Variant PRC1 Complex-Dependent H2A Ubiquitylation Drives PRC2 Recruitment and Polycomb Domain Formation (2014, background): “In contrast, PRC1 monoubiquitylates histone H2A on lysine 119 (H2AK119ub1) (de Napoles et al., 2004; Wang et al., 2004a).”
Histone Modifications and Cancer. (2016, background): “…of H2A at Lys119, incidentally, is also involved in transcriptional repression via PRC proteins, such as the RING1A and 1B ubiquitin ligases (de Napoles et al. 2004; Fang 14 Cite this article as Cold Spring Harb Perspect Biol 2016;8:a019521 ISWI Nonhomologous end joining Ub 53B P…”
Transcriptional regulation by Polycomb group proteins (2013, background): “; and from the Novo Nordisk Foundation, the Danish Cancer Society and the Danish Council for Strategic Research (12-110503) to K.”
The physics of epigenetics (2015, background): “C), histone ubiquitination and polycomb proteins are mechanistically related to propagate the silenced state (de Napoles et al., 2004).”
Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. (2005, background): “Interest-ingly, PRC1-mediated H2A ubiquitylation has also been linked to X inactivation (de Napoles et al., 2004; Fang et al., 2004).”