The emerging role of lysine methyltransferase SETD8 in human diseases

被引：70
|
作者：
Milite, Ciro [1 ,2 ]
Feoli, Alessandra [1 ,2 ,3 ]
Viviano, Monica [1 ,2 ]
Rescigno, Donatella [1 ,2 ,3 ]
Cianciulli, Agostino [1 ,2 ,3 ]
Balzano, Amodio Luca [1 ,2 ,3 ]
Mai, Antonello [4 ]
Castellano, Sabrina [1 ,2 ,5 ]
Sbardella, Gianluca [1 ,2 ]
机构：
[1] Univ Salerno, Dipartimento Farm, Via Giovanni Paolo 2 132, I-84084 Salerno, Italy
[2] Univ Salerno, Epigenet Med Chem Lab, Via Giovanni Paolo 2 132, I-84084 Salerno, Italy
[3] Univ Salerno, Programma Dottorato Ric Sci Farmaco, Via Giovanni Paolo 2 132, I-84084 Salerno, Italy
[4] Sapienza Univ Roma, Dipartimento Chim & Tecnol Farmaco, Ist Pasteur, Fdn Cenci Bolognetti, Ple A Moro 5, I-00185 Rome, Italy
[5] Univ Salerno, Dipartimento Med & Chirurg, Via Salvador Allende, I-84081 Salerno, Italy
来源：
CLINICAL EPIGENETICS | 2016年 / 8卷
关键词：
SMALL-MOLECULE INHIBITORS; 3' UNTRANSLATED REGION; MIR-502; BINDING-SITE; HISTONE H4-LYSINE 20; ACIDS B-E; CELL-CYCLE; PROTEIN METHYLTRANSFERASES; COMPETITIVE INHIBITOR; MIR-502-BINDING SITE; MARINE SEDIMENT;
D O I：
10.1186/s13148-016-0268-4
中图分类号：
R73 [肿瘤学];
学科分类号：
100214 ;
摘要：
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.
引用
收藏
页数：15
相关论文
共 50 条
  • [41] Downregulation of SETD8 by miR-382 is involved in glioma progression
    Ma, Zhiming
    PATHOLOGY RESEARCH AND PRACTICE, 2018, 214 (03) : 356 - 360
  • [42] Using cancer-associated variants to dissect functions of SETD8
    Zhu, Yongxia
    Wang, Lihui
    Senevirathne, Chamara
    Chen, Shi
    Silva, Fabio Pittella
    Luo, Minkui
    CANCER RESEARCH, 2018, 78 (13)
  • [43] SETD8 Staining in Plasma Cell Myeloma is Associated with Tumor Aggressiveness
    Salib, Christian
    Parekh, Samir
    Teruya-Feldstein, Julie
    MODERN PATHOLOGY, 2020, 33 (SUPPL 2) : 1376 - 1378
  • [44] SETD8 inhibits ferroptosis in pancreatic cancer by inhibiting the expression of RRAD
    Lu, Zekun
    Hu, Qiangsheng
    Qin, Yi
    Yang, Hao
    Xiao, Bingkai
    Chen, Weibo
    Ji, Shunrong
    Zu, Guangchen
    Wang, Zhiliang
    Fan, Guixiong
    Xu, Xiaowu
    Chen, Xuemin
    CANCER CELL INTERNATIONAL, 2023, 23 (01)
  • [45] The Use of Nucleosome Substrates Improves Binding of SAM Analogs to SETD8
    Strelow, John M.
    Xiao, Min
    Cavitt, Rachel N.
    Fite, Nathan C.
    Margolis, Brandon J.
    Park, Kyu-Jin
    JOURNAL OF BIOMOLECULAR SCREENING, 2016, 21 (08) : 786 - 794
  • [46] Lysine methyltransferase SETD6 modifies histones on a glycine-lysine motif
    Binda, Olivier
    EPIGENETICS, 2020, 15 (1-2) : 26 - 31
  • [47] MicroRNA-127-3p inhibits proliferation and invasion by targeting SETD8 in human osteosarcoma cells
    Zhang, Jun
    Hou, Wengen
    Chai, Mingxiang
    Zhao, Hongxing
    Jia, Jinling
    Sun, Xiaohui
    Zhao, Bin
    Wang, Ran
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2016, 469 (04) : 1006 - 1011
  • [48] LUNG SETD8 MRNA EXPRESSION PEAKS DURING ALVEOLAR FORMATION IN THE RAT
    Zhao, J. T.
    Yang, Y.
    Knecht, R.
    Joss-Moore, L.
    JOURNAL OF INVESTIGATIVE MEDICINE, 2016, 64 (01) : 342 - 342
  • [49] A Systematic Review to Define the Multi-Faceted Role of Lysine Methyltransferase SETD7 in Cancer
    Monteiro, Fatima Liliana
    Williams, Cecilia
    Helguero, Luisa A.
    CANCERS, 2022, 14 (06)
  • [50] SETD8 promotes stemness characteristics and is a potential prognostic biomarker of gastric adenocarcinoma
    Piao, Lihua
    Che, Nan
    Li, Haoyue
    Li, Mengxuan
    Feng, Ying
    Liu, Xingzhe
    Kim, Seokhyung
    Jin, Yu
    Xuan, Yanhua
    EXPERIMENTAL AND MOLECULAR PATHOLOGY, 2020, 117
12345