title: Diverse involvement of EZH2 in cancer epigenetics.
abstract: EZH2 is the catalytic subunit of Polycomb Repressor Complex 2 (PRC2) which catalyzes methylation of histone H3 at lysine 27 (H3K27me) and mediates gene silencing of target genes via local chromatin reorganization. Numerous evidences show that EZH2 plays a critical role in cancer initiation, progression and metastasis, as well as in cancer stem cell biology. Indeed, EZH2 dysregulation alters gene expression programs in various cancer types. The molecular mechanisms responsible for EZH2 alteration appear to be diverse and depending on the type of cancer. Furthermore, accumulating evidences indicate that EZH2 could also act as a PRC2-independent transcriptional activator in cancer. In this review, we address the current understanding of the oncogenic role of EZH2, including the mechanisms of EZH2 dysregulation in cancer and progresses in therapeutic approaches targeting EZH2.
authors.affiliation: Cell Plasticity & Cancer - Inserm U908, University of Lille Bâtiment SN3, Cité Scientifique, F-59655 Villeneuve d'Ascq, France ; Interdisciplinary Research Institute - CNRS USR3078/University of Lille Parc de la Haute Borne, 50 avenue de Halley, F-59658 Villeneuve d'Ascq, France.
authors.forename: Pamela
authors.initials: P
authors.lastname: Völkel
authors.affiliation: Cell Plasticity & Cancer - Inserm U908, University of Lille Bâtiment SN3, Cité Scientifique, F-59655 Villeneuve d'Ascq, France.
authors.forename: Barbara
authors.initials: B
authors.lastname: Dupret
authors.affiliation: Cell Plasticity & Cancer - Inserm U908, University of Lille Bâtiment SN3, Cité Scientifique, F-59655 Villeneuve d'Ascq, France.
authors.forename: Xuefen
authors.initials: X
authors.lastname: Le Bourhis
authors.affiliation: Cell Plasticity & Cancer - Inserm U908, University of Lille Bâtiment SN3, Cité Scientifique, F-59655 Villeneuve d'Ascq, France.
authors.forename: Pierre-Olivier
authors.initials: PO
authors.lastname: Angrand
keywords: EZH2; cancer; cancer stem cells; chromatin modification; histone lysine methylation; polycomb repression