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Nakagawa M, Kitabayashi I. Oncogenic roles of enhancer of zeste homolog 1/2 in hematological malignancies. Cancer Sci. 2018;109:2342--2348. 10.1111/cas.13655 1. INTRODUCTION {#cas13655-sec-0001} =============== Epigenetic regulation by DNA methylation, histone modifications, and non‐coding RNAs modulates gene expression without affecting DNA base sequences. Because aberrant DNA methylation or histone modifications are present in many malignant tumors, epigenetic dysregulation is considered a cause of tumor progression. Polycomb group (PcG) proteins regulate the expression of target genes by modulating histone modifications and are representative epigenetic regulators that maintain the "stemness" of embryonic and hematopoietic stem cells (HSC). Dysregulation of PcG proteins associated with mutations or gene overexpression is positively correlated with tumor progression in many hematological malignancies. In this review, we summarize the current knowledge of PcG proteins, focusing on the function of the histone methyltransferases enhancer of zeste homolog 1 and 2 (EZH1/2), which are subunits of polycomb repressive complexes (PRC), in hematological malignancies. In addition, we introduce novel therapeutic drugs for targeting these enzymes. 2. FUNCTION OF PRC {#cas13655-sec-0002} ================== The basic structural unit of chromatin consists of DNA wrapped around histone proteins. Histone proteins have an N‐terminal region termed the histone tail, which undergoes various chemical modifications including acetylation, methylation, phosphorylation, and ubiquitination. These chemical modifications contribute to the regulation of target gene expression by modifying the spatial structure of chromatin. PcG proteins play an important role in maintaining the transcriptional repression of target genes. PcG genes were first identified for their role in regulating the expression of homeotic genes, which control the body plan of embryos along the longitudinal axis and segmentation in *Drosophila*.[1](#cas13655-bib-0001){ref-type="ref"} PcG proteins form PRC in the nucleus. PRC are classified into PRC1 and PRC2 according to their biological characteristics. The core subunits of the mammalian PRC2 complex include EZH1/2, SUZ12, RbAp46/48, and EED. EZH1/2, which are histone methyltransferases, trimethylate histone H3 at lysine 27 (H3K27).[2](#cas13655-bib-0002){ref-type="ref"}, [3](#cas13655-bib-0003){ref-type="ref"} SUZ12 and EED activate methyltransferases and recruit PRC2 to the nucleosome, respectively.[4](#cas13655-bib-0004){ref-type="ref"}, [5](#cas13655-bib-0005){ref-type="ref"} The histone modification H3K27me3 represses target genes and mediates the recruitment of PRC1 to the nucleosome by serving as a docking site for the PRC1 component CBX (Figure [1](#cas13655-fig-0001){ref-type="fig"}A). PRC1 functions in transcriptional repression by catalyzing the monoubiquitination of histone H2A at lysine 119 (H2AK119). H2A ubiquitination blocks RNA polymerase II‐mediated transcriptional elongation.[6](#cas13655-bib-0006){ref-type="ref"} In addition, PRC1 induces chromatin condensation, which also contributes to the transcriptional repression of target genes. PRC1 complexes have 4 subunits, including Ring1A/B, CBX, PCGF, and PHC. Ring1A/B has ubiquitin ligase activity and ubiquitinates H2AK119.[7](#cas13655-bib-0007){ref-type="ref"} CBX is a chromodomain protein that recognizes H3K27me3 and recruits PRC1 to the nucleosome.[8](#cas13655-bib-0008){ref-type="ref"} PCGF (MEL18, BMI1) is a cofactor of Ring1A/B, and promotes its ubiquitin ligase activity.[9](#cas13655-bib-0009){ref-type="ref"} A non‐canonical PRC1 complex composed of RYBP and KDM2B, but not CBX, was recently identified and shown to target genes and ubiquitinate H2AK119 independently of PRC2 (Figure [1](#cas13655-fig-0001){ref-type="fig"}B).[10](#cas13655-bib-0010){ref-type="ref"}, [11](#cas13655-bib-0011){ref-type="ref"}, [12](#cas13655-bib-0012){ref-type="ref"} H2AK119ub1 recruits PRC2 to target genes and induces H3K27 trimethylation.[13](#cas13655-bib-0013){ref-type="ref"}, [14](#cas13655-bib-0014){ref-type="ref"} Canonical and non‐canonical PRC1 complexes have similar activity in the ubiquitination of H2A in a PRC2‐dependent or ‐independent method, resulting