ArticleChembiochem : a European journal of chemical biology2020
Analysis of the Substrate Specificity of the SMYD2 Protein Lysine Methyltransferase and Discovery of Novel Non-Histone Substrates.
Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- The Olive PhenolicNutrients · 2025Article
- A Novel Inhibitor of Methyltransferase SMYD2, AZ505 Protects Against Peritoneal Fibrosis in Mice.Clinical and experimental pharmacology & physiology · 2025Article
- Role of SMYD2 in gastrointestinal cancer progression (Review).Oncology letters · 2025Review
- Emergent properties of the lysine methylome reveal regulatory roles via protein interactions and histone mimicry.Epigenomics · 2025Article
- Distinct specificities of the HEMK2 protein methyltransferase in methylation of glutamine and lysine residues.Protein science : a publication of the Protein Society · 2024Article
- The homeoprotein HOXB2 limits triple-negative breast carcinogenesis via extracellular matrix remodeling.International journal of biological sciences · 2024Article
- Mechanistic and functional extrapolation of SET and MYND domain-containing protein 2 to pancreatic cancer.World journal of gastroenterology · 2022Review
- Lysine methyltransferase inhibitors: where we are now.RSC chemical biology · 2022Review
- How Protein Methylation Regulates Steroid Receptor Function.Endocrine reviews · 2022Review
- Specificity Analysis of Protein Methyltransferases and Discovery of Novel Substrates Using SPOT Peptide Arrays.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Pharmacological inhibition of SMYD2 protects against cisplatin-induced acute kidney injury in mice.Frontiers in pharmacology · 2022Article
- Analysis of the Substrate Specificity of the SMYD2 Protein Lysine Methyltransferase and Discovery of Novel Non-Histone Substrates.Chembiochem : a European journal of chemical biology · 2020Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
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Abstract
The SMYD2 protein lysine methyltransferase methylates various histone and non-histone proteins and is overexpressed in several cancers. Using peptide arrays, we investigated the substrate specificity of the enzyme, revealing a recognition of leucine (or weaker phenylalanine) at the -1 peptide site and disfavor of acidic residues at the +1 to +3 sites. Using this motif, novel SMYD2 peptide substrates were identified, leading to the discovery of 32 novel peptide substrates with a validated target site. Among them, 19 were previously reported to be methylated at the target lysine in human cells, strongly suggesting that SMYD2 is the protein lysine methyltransferase responsible for this activity. Methylation of some of the novel peptide substrates was tested at the protein level, leading to the identification of 14 novel protein substrates of SMYD2, six of which were more strongly methylated than p53, the best SMYD2 substrate described so far. The novel SMYD2 substrate proteins are involved in diverse biological processes such as chromatin regulation, transcription, and intracellular signaling. The results of our study provide a fundament for future investigations into the role of this important enzyme in normal development and cancer.
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