Lung cancer is one of the most common malignancies. In spite of the progress made in past decades, further studies to improve current therapy for lung cancer are required. Dynamically controlled by methyltransferases and demethylases, methylation of lysine and arginine residues on histone proteins regulates chromatin organization and thereby gene transcription. Aberrant alterations of histone methylation have been demonstrated to be associated with the progress of multiple cancers including lung cancer. Inhibitors of methyltransferases and demethylases have exhibited anti-tumor activities in lung cancer, and multiple lead candidates are under clinical trials. Here, we summarize how histone methylation functions in lung cancer, highlighting most recent progresses in small molecular inhibitors for lung cancer treatment.
Keywords: ALK, anaplastic lymphoma kinase; DUSP3, dual-specificity phosphatase 3; EMT, epithelial-to-mesenchymal transition; Elk1, ETS-domain containing protein; HDAC, histone deacetylase; Histone demethylase; Histone demethylation; Histone methylation; Histone methyltransferase; IHC, immunohistochemistry; Inhibitors; KDMs, lysine demethylases; KLF2, Kruppel-like factor 2; KMTs, lysine methyltransferases; LSDs, lysine specific demethylases; Lung cancer; MEP50, methylosome protein 50; NSCLC, non-small cell lung cancer; PAD4, peptidylarginine deiminase 4; PCNA, proliferating cell nuclear antigen; PDX, patient-derived xenografts; PRC2, polycomb repressive complex 2; PRMTs, protein arginine methyltrasferases; PTMs, posttranslational modifications; SAH, S-adenosyl-L-homocysteine; SAM, S-adenosyl-L-methionine; SCLC, small cell lung cancer; TIMP3, tissue inhibitor of metalloproteinase 3.