Structure, Activity, and Function of the Protein Lysine Methyltransferase G9a - Centre de recherche en cancérologie de Lyon (UMR INSERM 1052 ; CNRS 5286 ; Centre Léon Bérard) Accéder directement au contenu
Article Dans Une Revue Life Année : 2021

Structure, Activity, and Function of the Protein Lysine Methyltransferase G9a

Résumé

G9a is a lysine methyltransferase catalyzing the majority of histone H3 mono- and dimethylation at Lys-9 (H3K9), responsible for transcriptional repression events in euchromatin. G9a has been shown to methylate various lysine residues of non-histone proteins and acts as a coactivator for several transcription factors. This review will provide an overview of the structural features of G9a and its paralog called G9a-like protein (GLP), explore the biochemical features of G9a, and describe its post-translational modifications and the specific inhibitors available to target its catalytic activity. Aside from its role on histone substrates, the review will highlight some non-histone targets of G9a, in order gain insight into their role in specific cellular mechanisms. Indeed, G9a was largely described to be involved in embryonic development, hypoxia, and DNA repair. Finally, the involvement of G9a in cancer biology will be presented.
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Dates et versions

hal-03870111 , version 1 (27-02-2024)

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Coralie Poulard, Lara Noureddine, Ludivine Pruvost, Muriel Le Romancer. Structure, Activity, and Function of the Protein Lysine Methyltransferase G9a. Life, 2021, 11 (10), pp.1082. ⟨10.3390/life11101082⟩. ⟨hal-03870111⟩
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