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Clin Epigenetics. 2016 Sep 22;8:102. eCollection 2016.

The emerging role of lysine methyltransferase SETD8 in human diseases.

Author information

1
Dipartimento di Farmacia, Università degli Studi di Salerno, Via Giovanni Paolo II 132, Fisciano, I-84084 Salerno, Italy ; Epigenetic Med Chem Lab, Università degli Studi di Salerno, Via Giovanni Paolo II 132, Fisciano, I-84084 Salerno, Italy.
2
Dipartimento di Farmacia, Università degli Studi di Salerno, Via Giovanni Paolo II 132, Fisciano, I-84084 Salerno, Italy ; Epigenetic Med Chem Lab, Università degli Studi di Salerno, Via Giovanni Paolo II 132, Fisciano, I-84084 Salerno, Italy ; Programma di Dottorato di Ricerca in Scienze del Farmaco, Università degli studi di Salerno, Via Giovanni Paolo II 132, Fisciano, I-84084 Salerno, Italy.
3
Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Chimica e Tecnologie del Farmaco, "Sapienza" Università di Roma, P.le A. Moro 5, I-00185 Rome, Italy.
4
Dipartimento di Farmacia, Università degli Studi di Salerno, Via Giovanni Paolo II 132, Fisciano, I-84084 Salerno, Italy ; Epigenetic Med Chem Lab, Università degli Studi di Salerno, Via Giovanni Paolo II 132, Fisciano, I-84084 Salerno, Italy ; Dipartimento di Medicina e Chirurgia, Università degli Studi di Salerno, Via Salvador Allende, Baronissi, I-84081 Salerno, Italy.

Abstract

SETD8/SET8/Pr-SET7/KMT5A is the only known lysine methyltransferase (KMT) that monomethylates lysine 20 of histone H4 (H4K20) in vivo. Lysine residues of non-histone proteins including proliferating cell nuclear antigen (PCNA) and p53 are also monomethylated. As a consequence, the methyltransferase activity of the enzyme is implicated in many essential cellular processes including DNA replication, DNA damage response, transcription modulation, and cell cycle regulation. This review aims to provide an overview of the roles of SETD8 in physiological and pathological pathways and to discuss the progress made to date in inhibiting the activity of SETD8 by small molecules, with an emphasis on their discovery, selectivity over other methyltransferases and cellular activity.

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