Critical roles of non-histone protein lysine methylation in human tumorigenesis
By Ryuji Hamamoto, V. Saloura, Yusuke Nakamura. 2015
345 citations recorded by the source corpus.
Subfields: Molecular Biology
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Molecular Biology
- Ryuji Hamamoto
- Yusuke Nakamura
- N. Dohmae
- Takehiro Suzuki
- Makoto Nakakido
- Lianhua Piao
- Zhenzhong Deng
- Yuichiro Yoshioka
Citations in the corpus
- WHSC1L1-mediated EGFR mono-methylation enhances the cytoplasmic and nuclear oncogenic activity of EGFR in head and neck cancer (2017, neutral): “Mounting evidence over the past decade supports that protein methylation regulates oncogenesis not only through histone modification, but also through methylation of non-histone substrates 30,31 .”
- The histone methyltransferase SMYD2 is a novel therapeutic target for the induction of apoptosis in ovarian clear cell carcinoma cells (2020, background): “Epigenetic mechanisms, such as histone modification, regulate gene expression by altering chromatin structure (5,6).”
- Protein lysine methyltransferase SMYD3 is involved in tumorigenesis through regulation of HER2 homodimerization (2017, background): “We previously reported that molecular functions of lysine methylation are classified into at least five different classes including one class to regulate further modification(s) of a substrate protein [13].”
- Oncogenic histone methyltransferase EZH2: A novel prognostic marker with therapeutic potential in endometrial cancer (2017, neutral): “Enzymes relevant to histone methylation and involved in human tumorigenesis have recently attracted attention for anti-cancer drug development [6].”
- SMYD3-mediated lysine methylation in the PH domain is critical for activation of AKT1 (2016, neutral): “A large body of literature and databases have documented frequent overexpression of SMYD3 (Supplementary Figures S2 and S3) and hyperactivation of the AKT pathway in a variety of malignancies [1, 11, 26].”
- Deregulation of the Histone Lysine-Specific Demethylase 1 Is Involved in Human Hepatocellular Carcinoma (2019, background): “These epigenetic changes caused by LSD1 have been shown to play a key role in human tumorigenesis [18,25,47].”
- SUV39H2 methylates and stabilizes LSD1 by inhibiting polyubiquitination in human cancer cells (2015, background): “Indeed, clinical trials of LSD1 inhibitors have just started for small cell lung carcinoma and acute myeloid leukemia [6].”
- Dysregulation of AKT Pathway by SMYD2-Mediated Lysine Methylation on PTEN (2015, background): “We and others reported that lysine methylation can affect the phosphorylation status of another amino acid in the same protein [34].”
- 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].”
- WHSC1L1 drives cell cycle progression through transcriptional regulation of CDC6 and CDK2 in squamous cell carcinoma of the head and neck (2016, neutral): “The Cancer Genome Atlas Consortium (TCGA) [3, 4] has revealed a plethora of genetic and expression alterations in a class of enzymes known as protein methyltransferases (PMTs) in many different cancer types, suggesting the importance of these enzymes in cancer development and progression [5].”
- Targeting Suppressor of Variegation 3-9 Homologue 2 (SUV39H2) in Acute Lymphoblastic Leukemia (ALL) (2015, background): “Furthermore, mutations in histone methyltransferase enhancer of zeste homologue 2 (EZH2) has been documented in a wide variety of B- and T-cell lymphoproliferative disorders [28,29].”
- Critical roles of SMYD2-mediated β-catenin methylation for nuclear translocation and activation of Wnt signaling (2017, background): “Since it is known that the majority of SMYD2 protein is located in the cytoplasm, we hypothesized that methylation of a lysine residue in β-catenin might affect its subcellular localization in cancer cells as we reported examples in our review [10, 11] and in turn, regulate the Wnt signaling pathway”
- PRMT1 promotes mitosis of cancer cells through arginine methylation of INCENP (2015, background): “Accumulated evidence has indicated that methylation of arginine and lysine residues plays an important role in the regulation of many biological processes like phosphorylation does, and its deregulation is almost certainly involved in human tumorigenesis [14, 35-37].”