{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSMYD2 is a versatile protein lysine methyltransferase that orchestrates key cellular processes by modifying both histone and non‐histone substrates. It methylates central tumor suppressors such as the retinoblastoma protein (RB) at conserved lysine residues (e.g. K860 and K810), and the tumor suppressor p53, preferentially at lysine 370, thereby impeding its transcriptional activity. In addition, SMYD2 mono‐methylates PARP1 at lysine 528 and PTEN at lysine 313, events that modulate the cellular DNA damage response and activate the PI3K–AKT signaling axis, respectively. Methylation of estrogen receptor α at lysine 266 further underscores its role in fine‐tuning hormone‐dependent transcription. Comprehensive proteomic analyses have established a wide interactome for SMYD2, while small molecule inhibitors (e.g. AZ505) have been used to validate its substrate specificity and functional relevance in cancer cells."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSMYD2’s oncogenic roles have been documented across a wide spectrum of malignancies. In gastric cancer, overexpression of SMYD2 drives tumor cell proliferation, while selective chemical probes (such as LLY‐507) diminish p53 methylation and impede cancer cell growth in esophageal, liver, and breast cancer models. Large‐scale proteomic studies have expanded its substrate repertoire in esophageal squamous cell carcinoma, and its catalytic activity underlies oncogenic signaling through methylation of proteins such as HSP90AB1, which modulates proper chaperone assembly. Moreover, SMYD2‐mediated methylation of transcriptional regulators including STAT3 and NF‐κB subunits contributes to aggressive breast cancer phenotypes, whereas its aberrant activity is linked to poor clinical outcomes in papillary thyroid carcinoma, colon cancer (via modulation of ERBB2/FUT4 signaling) and glioma. In hepatocellular carcinoma, SMYD2 methylates c‐Myc to stabilize the oncoprotein and promote glutamine metabolic reprogramming."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its oncogenic functions, SMYD2 is emerging as a critical regulator in diverse physiological processes and a promising therapeutic target. It influences viral latency by depositing repressive chromatin marks at the HIV‐1 promoter and promotes differentiation of human embryonic stem cells toward mesendoderm lineages. Structural and computational studies have elucidated its substrate binding determinants while revealing a broad specificity that accommodates multiple targets—including methylation of EZH2, which enhances its protein stability and repressive function. Comprehensive reviews further highlight the potential of pharmacologically targeting SMYD2 and its SMYD family counterparts, with recent work demonstrating that SMYD2 inhibition downregulates TMPRSS2 to curtail SARS‐CoV‐2 replication and modulates osteoblast differentiation via interplay with Ezh2."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Mohamed Abu-Farha, Jean-Philippe Lambert, Ashraf S Al-Madhoun, et al. 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