MLL targets SET domain methyltransferase activity to Hox gene promoters.

By T. Milne, S. Briggs, H. Brock, MaryEllen Martin, Denise Gibbs, C. D. Allis, J. Hess. Molecules and Cells, 2002

1,136 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/747529e9b8d77999209fe3cf0519754b778d3d52

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Citations in the corpus

Histone methylation by PRC2 is inhibited by active chromatin marks. (2011, background): “Among the trxG proteins that keep PcG target genes active are the HMTases Trx and Ash1, which methylate H3K4 and H3K36, respectively (Milne et al., 2002; Nakamura et al., 2002; Tanaka et al., 2007).”
Histone and chromatin cross-talk. (2003, background): “Moreover, acetylation on H3-K9 and H3-K14 stimulates methylation of H3-K4 by the HMT, MLL (mixed lineage leukemia protein) [29].”
Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. (2003, background): “MLL/ALL is a componentsition between initiation and elongation, and Set1 inof an H3-K4 methylase that is recruited to active Hoxteracts with the form of Pol II whose CTD is phosphorypromoters (Milne et al., 2002; Nakamura et al., 2002).lated at serine 5 but not serine 2.”
The menin tumor suppressor protein is an essential oncogenic cofactor for MLL-associated leukemogenesis. (2005, background): “MLL possesses inherent histone methyltransferase (HMT) activity, which is specific for lysine 4 of histone H3 (H3K4) (Milne et al., 2002; Nakamura et al., 2002), a mark that is generally associated with transcriptionally active states of chromatin (Noma et al., 2001; Strahl et al., 1999), thus…”
The functions of E(Z)/EZH2-mediated methylation of lysine 27 in histone H3. (2004, background): “Recent demonstrations that members of PcG and trxG proteins contain intrinsic histone methyltransferase (HMTase) activity raise the possibility that PcG and trxG proteins participate in cellular memory through methylating core histones [11,12 (cid:2)(cid:2) –15 (cid:2)(cid:2) ,16,17].”
Covalent histone modifications: miswritten, misinterpreted, and miserased in human cancers (2010, background): “, and was later shown to encode a major H3K4-specific HMT enzym”
The SET-domain protein superfamily: protein lysine methyltransferases (2005, background): “MLL1, the human homolog of Drosophila Trx and a member of the SET1 family, is often implicated in leukemia as a result of aberrant Hox gene activation mediated by histone H3 K4 methylation [45].”
Leukemia Proto-Oncoprotein MLL Forms a SET1-Like Histone Methyltransferase Complex with Menin To Regulate Hox Gene Expression (2004, neutral): “associated with transcriptionally active chromatin (42, 44).”
Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. (2005, background): “…EED-EZH2 complex possess H3-K27 methyltransferase activity (Beisel et al., 2002; Cao et al., 2002; Czermin et al., 2002; Kuzmichev et al., 2002; Milne et al., 2002; Muller et al., 2002; Nakamura et al., 2002), the PRC1 complex has been recently demonstrated to possess H2A-K119 ubiquitin E3…”
SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells (2004, background): “MLL activates transcription of the Ho x gene through H3-K4-specific methylation, which is mediated by the methylase activity of the SET domai”
Elongation by RNA polymerase II: the short and long of it. (2004, background): “Only recently was it determined that MLL, and its related proteins, function as histone methyltransferases (Milne et al. 2002; Nakamura et al. 2002).”
SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex. (2004, background): “…methylation of core histones (Beisel et al., 2002; Cao et H3-K27 methylation was also demonstrated to partici-al., 2002; Czermin et al., 2002; Kuzmichev et al., 2002; pate in X inactivation (Plath et al., 2003; Silva et al., Milne et al., 2002; Muller et al., 2002; Nakamura et al., 2003).”