Repression of p53 activity by Smyd2-mediated methylation

By Jing Huang, Laura Pérez-Burgos, B. Placek, Roopsha Sengupta, Mario Richter, Jean A. Dorsey, S. Kubicek, Susanne Opravil, T. Jenuwein, S. Berger. Nature, 2006

622 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/35cd66c3835e149e3475ae720729a18d0d63a44a

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Citations in the corpus

Histone Modifications and Cancer. (2016, background): “Among the many known examples are HDAC6, SIRT1, SIRT2, SET7/9, SETD8, SMYD2, PRMT5, and EHMT2/G9a) (Hubbert et al. 2002; Huang et al. 2006; Shi et al. 2007; Pradhan et al. 2009; Karkhanis et al. 2011; Stunkel and Campbell 2011).”
Dysregulation of AKT Pathway by SMYD2-Mediated Lysine Methylation on PTEN (2015, background): “Although SMYD2 was originally identified as a histone methyltransferase that specifically methylates H3K36 [39], recent studies identified various non-histone protein substrates of SMYD2 such as p53, retinoblastoma 1, heat shock protein 90kDa, estrogen receptor alpha, and poly (ADP-ribose) polymeras”
Methylation multiplicity and its clinical values in cancer (2021, neutral): “79).”
Phosphorylation of EZH2 activates STAT3 signaling via STAT3 methylation and promotes tumorigenicity of glioblastoma stem-like cells (2013, background): “A series of reports showed that histone methyltransferases such as SET7/9 can regulate signaling pathways through direct methylation of p53, NF-kB, and STAT3 (Huang et al., 2006; Lu et al., 2010; Stark et al., 2011; Yang et al., 2010), raising the possibility that EZH2 might have such a property.”
RB1 methylation by SMYD2 enhances cell cycle progression through an increase of RB1 phosphorylation. (2012, background): “Besides histone methylation process, SMYD2 also methylates p53 and altering their functions [10].”
Understanding the language of Lys36 methylation at histone H3 (2012, background): “In addition to targeting H3K36, SMYD2 methylates H3K4 and non-histone substrates, such as p53 and retinoblastoma (RB”
SMYD2-dependent HSP90 methylation promotes cancer cell proliferation by regulating the chaperone complex formation. (2014, background): “293T cells were co-transfected with a FLAGSMYD2 expression vector and four different lengths of HA-HSP90AB1 vectors ([1–724], [1–500], [250–724] and [500–724]).”
Blinded by the Light: The Growing Complexity of p53. (2009, background): “Methylation of K372 by the SET domain methyltransferase Set9 leads to increased p21 expression (Chuikov et al., 2004), but whether this has a selective impact on p53 target gene activation has not been determined.”
The histone methyltransferase SMYD2 methylates PARP1 and promotes poly(ADP-ribosyl)ation activity in cancer cells. (2014, background): “SMYD2 is also known to methylate non-histone protein substrates, including p53 and RB1, and methylated p53 was reported to lose its tumor suppressive function [29,30].”
Enhanced HSP70 lysine methylation promotes proliferation of cancer cells through activation of Aurora kinase B (2012, neutral): “IB: HA (AURKB) HA–AURKB – – + – + – FLAG–AURKB-[1-200] FLAG–AURKB-[201-344]”
The histone methyltransferase SMYD2 is a novel therapeutic target for the induction of apoptosis in ovarian clear cell carcinoma cells (2020, background): “It has been demonstrated that SMYD2 could attenuate the tumor suppressive function of p53 through methylation of Lys370 in the H1299 cell line, which is a human non‐small cell lung carcinoma cell line (12).”
The lysine 831 of vascular endothelial growth factor receptor 1 is a novel target of methylation by SMYD3. (2007, background): “17). In addition, methylation of p53 K370 has been shown by SMYD2, another member of the SMYD (SET and MYND domain) family ( 19 ).”