Enhanced SMYD3 expression is essential for the growth of breast cancer cells

By Ryuji Hamamoto, F. P. Silva, M. Tsuge, Toshihiko Nishidate, T. Katagiri, Yusuke Nakamura, Yoichi Furukawa. 2006

265 citations recorded by the source corpus.

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In Molecular Biology

Citations in the corpus

RB1 methylation by SMYD2 enhances cell cycle progression through an increase of RB1 phosphorylation. (2012, background): “We previously showed that some histone methyltransferases (HMTs) play vital roles in human cancer pathogenesis [22,34–36].”
Enhanced expression of EHMT2 is involved in the proliferation of cancer cells through negative regulation of SIAH1. (2011, background): “We previously reported that the histone methyltransferase SMYD3 stimulates cell proliferation through its methyltransferase activity and plays a crucial role in human carcinogenesis [7,8], and several groups also showed that deregulation of histone methyltransferases could be involved in human carci”
Enhanced HSP70 lysine methylation promotes proliferation of cancer cells through activation of Aurora kinase B (2012, unknown): “IB: HA (AURKB) HA–AURKB – – + – + – FLAG–AURKB-[1-200] FLAG–AURKB-[201-344]”
SUV39H2 methylates and stabilizes LSD1 by inhibiting polyubiquitination in human cancer cells (2015, background): “Many reports have indicated that dysregulation of protein lysine methyltransferases and protein lysine demethylases has important roles in human tumorigenesis [32-37].”
Late Cornified Envelope Group I, a Novel Target of p53, Regulates PRMT5 Activity (2014, methodology): “HEK293T cells were transfected with HA-Mock (empty vector of pCAGGSnHC) or HALCE1F (pCAGGSnHC-LCE1F) using FuGENE6.”
Enhanced methyltransferase activity of SMYD3 by the cleavage of its N-terminal region in human cancer cells (2008, background): “We showed in our earlier studies that the expression levels of SMYD3 protein are elevated in human hepatocellular carcinoma (HCC), colorectal carcinoma (CRC) and breast cancer (Hamamoto et al., 2004, 2006).”
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]).”
Histone lysine methyltransferase SETD8 promotes carcinogenesis by deregulating PCNA expression. (2012, methodology): “FLAGPCNA (WT) or FLAG-PCNA (K248A) and HA-SETD8 (1-352) expression vectors were transfected into 293T cells together with an HA-Ubiquitin or an HA-Mock expression vector.”
PRMT6 increases cytoplasmic localization of p21CDKN1A in cancer cells through arginine methylation and makes more resistant to cytotoxic agents (2015, background): “Indeed, dysregulation of arginine and lysine methyltransferases have frequently been observed in human cancer [38–43], and these enzymes are now considered as emergent targets for anti-cancer drug development [14, 39, 44].”
The histone methyltransferase SMYD2 methylates PARP1 and promotes poly(ADP-ribosyl)ation activity in cancer cells. (2014, background): “The accumulated evidence implicates deregulation of histone methylation appears to play crucial roles in human carcinogenesis [21]; for example, many lysine methyltransferases have been shown to function as oncogenes [22-26].”
SMYD3-mediated lysine methylation in the PH domain is critical for activation of AKT1 (2016, unknown): “In fact, overexpression of SMYD3 is observed in a wide variety of cancer tissues [10–12] (Supplementary Figures S2 and S3), and inactivation of SMYD3 results in growth suppression of various types of cancer cells (Supplementary Figure S10) [10, 12].”
Overexpression of the JmjC histone demethylase KDM5B in human carcinogenesis: involvement in the proliferation of cancer cells through the E2F/RB pathway (2010, background): “We previously reported that SMYD3, a histone methyltransferase, stimulates cell proliferation through its methyltransferase activity and plays a crucial role in human carcinogenesis [6-10].”
The lysine 831 of vascular endothelial growth factor receptor 1 is a novel target of methylation by SMYD3. (2007, background): “In our earlier studies, we reported that SMYD3 has dimethyltransferase and trimethyltransferase activity on H3K4, and that elevated SMYD3 expression plays a crucial role in the proliferation of colorectal carcinoma, hepatocellular carcinoma, and breast cancer cells (7, 15 ); overexpression of SMYD3”