Regulation and function of histone acetyltransferase MOF

doi:10.1007/s11684-014-0314-6

Front Med

2014, Vol. 8

Issue (1) : 79-83 https://doi.org/10.1007/s11684-014-0314-6

REVIEW

Regulation and function of histone acetyltransferase MOF

Yang Yang, Xiaofei Han, Jingyun Guan, Xiangzhi Li(

)

Key Laboratory of Experimental Teratology, Ministry of Education, Department of Cell Biology, Shandong University School of Medicine, Jinan 250012, China

Download: PDF(146 KB) HTML
Export: BibTeX | EndNote | Reference Manager | ProCite | RefWorks

Abstract

The mammalian MOF (male absent on the first), a member of the MYST (MOZ, YBF2, SAS2, and Tip60) family of histone acetyltransferases (HATs), is the major enzyme that catalyzes the acetylation of histone H4 on lysine 16. Acetylation of K16 is a prevalent mark associated with chromatin decondensation. MOF has recently been shown to play an essential role in maintaining normal cell functions. In this study, we discuss the important roles of MOF in DNA damage repair, apoptosis, and tumorigenesis. We also analyze the role of MOF as a key regulator of the core transcriptional network of embryonic stem cells.

Keywords MOF histone acetyltransferase DNA damage repair tumorigenesis embryonic stem cells

Corresponding Author(s): Li Xiangzhi,Email:xiangzhi@sdu.edu.cn

Issue Date: 26 April 2014

Cite this article:

Yang Yang,Xiaofei Han,Jingyun Guan, et al. Regulation and function of histone acetyltransferase MOF[J]. Front Med, 2014, 8(1): 79-83.

URL:

https://academic.hep.com.cn/fmd/EN/10.1007/s11684-014-0314-6
https://academic.hep.com.cn/fmd/EN/Y2014/V8/I1/79

Fig.1 MOF is a HAT that acetylates chromatin mostly at histone H4 lysine 16 (H4K16).

Fig.2 MOF is required for ESC self-renewal and differentiation.

1	Morales V, Straub T, Neumann MF, Mengus G, Akhtar A, Becker PB. Functional integration of the histone acetyltransferase MOF into the dosage compensation complex. EMBO J 2004; 23(11): 2258–2268 doi: 10.1038/sj.emboj.7600235 pmid:15141166
2	Smith ER, Cayrou C, Huang R, Lane WS, C?té J, Lucchesi JC. A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16. Mol Cell Biol 2005; 25(21): 9175–9188 doi: 10.1128/MCB.25.21.9175-9188.2005 pmid:16227571
3	Li X, Wu L, Corsa CA, Kunkel S, Dou Y. Two mammalian MOF complexes regulate transcription activation by distinct mechanisms. Mol Cell 2009; 36(2): 290–301 doi: 10.1016/j.molcel.2009.07.031 pmid:19854137
4	Conrad T, Akhtar A. Dosage compensation in Drosophila melanogaster: epigenetic fine-tuning of chromosome-wide transcription. Nat Rev Genet 2012; 13(2): 123–134 doi: 10.1038/nrg3124 pmid:22251873
5	Gelbart ME, Kuroda MI. Drosophila dosage compensation: a complex voyage to the X chromosome. Development 2009; 136(9): 1399–1410 doi: 10.1242/dev.029645 pmid:19363150
6	Lucchesi JC, Kelly WG, Panning B. Chromatin remodeling in dosage compensation. Annu Rev Genet 2005; 39(1): 615–651 doi: 10.1146/annurev.genet.39.073003.094210 pmid:16285873
7	Taipale M, Rea S, Richter K, Vilar A, Lichter P, Imhof A, Akhtar A. hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells. Mol Cell Biol 2005; 25(15): 6798–6810 doi: 10.1128/MCB.25.15.6798-6810.2005 pmid:16024812
8	Hilfiker A, Hilfiker-Kleiner D, Pannuti A, Lucchesi JC. mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to the SAS genes of yeast, is required for dosage compensation in Drosophila. EMBO J 1997; 16(8): 2054–2060 doi: 10.1093/emboj/16.8.2054 pmid:9155031
9	Gupta A, Guerin-Peyrou TG, Sharma GG, Park C, Agarwal M, Ganju RK, Pandita S, Choi K, Sukumar S, Pandita RK, Ludwig T, Pandita TK. The mammalian ortholog of Drosophila MOF that acetylates histone H4 lysine 16 is essential for embryogenesis and oncogenesis. Mol Cell Biol 2008; 28(1): 397–409 doi: 10.1128/MCB.01045-07 pmid:17967868
10	Li X, Corsa CA, Pan PW, Wu L, Ferguson D, Yu X, Min J, Dou Y. MOF and H4 K16 acetylation play important roles in DNA damage repair by modulating recruitment of DNA damage repair protein Mdc1. Mol Cell Biol 2010; 30(22): 5335–5347 doi: 10.1128/MCB.00350-10 pmid:20837706
11	Dou Y, Milne TA, Tackett AJ, Smith ER, Fukuda A, Wysocka J, Allis CD, Chait BT, Hess JL, Roeder RG. Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell 2005; 121(6): 873–885 doi: 10.1016/j.cell.2005.04.031 pmid:15960975
12	Thomas T, Dixon MP, Kueh AJ, Voss AK. Mof (MYST1 or KAT8) is essential for progression of embryonic development past the blastocyst stage and required for normal chromatin architecture. Mol Cell Biol 2008; 28(16): 5093–5105 doi: 10.1128/MCB.02202-07 pmid:18541669
13	Li X, Dou Y. New perspectives for the regulation of acetyltransferase MOF. Epigenetics 2010; 5(3): 185–188 doi: 10.4161/epi.5.3.11372 pmid:20305383
16	Li X, Li L, Pandey R, Byun JS, Gardner K, Qin Z, Dou Y. The histone acetyltransferase MOF is a key regulator of the embryonic stem cell core transcriptional network. Cell Stem Cell 2012; 11(2): 163–178 doi: 10.1016/j.stem.2012.04.023 pmid:22862943
17	Sun B, Guo S, Tang Q, Li C, Zeng R, Xiong Z, Zhong C, Ding J. Regulation of the histone acetyltransferase activity of hMOF via autoacetylation of Lys274. Cell Res 2011; 21(8): 1262–1266 doi: 10.1038/cr.2011.105 pmid:21691301
18	Yang C, Wu J, Sinha SH, Neveu JM, Zheng YG. Autoacetylation of the MYST lysine acetyltransferase MOF protein. J Biol Chem 2012; 287(42): 34917–34926 doi: 10.1074/jbc.M112.359356 pmid:22918831
19	Yuan H, Rossetto D, Mellert H, Dang WW, Srinivasan M, Johnson J, Hodawadekar S, Ding EC, Speicher K, Abshiru N, Perry R, Wu J, Yang C, Zheng YG, Speicher DW, Thibault P, Verreault A, Johnson FB, Berger SL, Sternglanz R, McMahon SB, C?té J, Marmorstein R. MYST protein acetyltransferase activity requires active site lysine autoacetylation. EMBO J 2012; 31(1): 58–70 doi: 10.1038/emboj.2011.382 pmid:22020126
20	Lu L, Li L, Lv X, Wu XS, Liu DP, Liang CC. Modulations of hMOF autoacetylation by SIRT1 regulate hMOF recruitment and activities on the chromatin. Cell Res 2011; 21(8): 1182–1195 doi: 10.1038/cr.2011.71 pmid:21502975
21	Peng LR, Ling HB, Yuan ZG, Fang B, Bloom G, Fukasawa K, Koomen J, Chen JD, Lane WS, Seto E. SIRT1 negatively regulates the activities, functions, and protein levels of hMOF and TIP60. Mol Cell Biol 2012; 32(14): 2823–2836 doi: 10.1128/MCB.00496-12 pmid:22586264
22	Katoh H, Qin ZS, Liu RH, Wang LZ, Li WQ, Li X, Wu LP, Du ZW, Lyons R, Liu CG, Liu X, Dou Y, Zheng P, Liu Y. FOXP3 orchestrates H4K16 acetylation and H3K4 trimethylation for activation of multiple genes by recruiting MOF and causing displacement of PLU-1. Mol Cell 2011; 44(5): 770–784 doi: 10.1016/j.molcel.2011.10.012 pmid:22152480
23	Gupta A, Sharma GG, Young CS, Agarwal M, Smith ER, Paull TT, Lucchesi JC, Khanna KK, Ludwig T, Pandita TK. Involvement of human MOF in ATM function. Mol Cell Biol 2005; 25(12): 5292–5305 doi: 10.1128/MCB.25.12.5292-5305.2005 pmid:15923642
24	Sharma GG, So S, Gupta A, Kumar R, Cayrou C, Avvakumov N, Bhadra U, Pandita RK, Porteus MH, Chen DJ, Cote J, Pandita TK. MOF and histone H4 acetylation at lysine 16 are critical for DNA damage response and double-strand break repair. Mol Cell Biol 2010; 30(14): 3582–3595 doi: 10.1128/MCB.01476-09 pmid:20479123
25	Taipale M, Akhtar A. Chromatin mechanisms in Drosophila dosage compensation. Prog Mol Subcell Biol 2005; 38: 123–149 doi: 10.1007/3-540-27310-7_5 pmid:15881893
26	Sykes SM, Mellert HS, Holbert MA, Li K, Marmorstein R, Lane WS, McMahon SB. Acetylation of the p53 DNA-binding domain regulates apoptosis induction. Mol Cell 2006; 24(6): 841–851 doi: 10.1016/j.molcel.2006.11.026 pmid:17189187
27	Mellert HS, Stanek TJ, Sykes SM, Rauscher FJ 3rd, Schultz DC, McMahon SB. Deacetylation of the DNA-binding domain regulates p53-mediated apoptosis. J Biol Chem 2011; 286(6): 4264–4270 doi: 10.1074/jbc.M110.184663 pmid:21148320
28	Sykes SM, Stanek TJ, Frank A, Murphy ME, McMahon SB. Acetylation of the DNA binding domain regulates transcription-independent apoptosis by p53. J Biol Chem 2009; 284(30): 20197–20205 doi: 10.1074/jbc.M109.026096 pmid:19494119
29	Fraga MF, Ballestar E, Villar-Garea A, Boix-Chornet M, Espada J, Schotta G, Bonaldi T, Haydon C, Ropero S, Petrie K, Iyer NG, Pérez-Rosado A, Calvo E, Lopez JA, Cano A, Calasanz MJ, Colomer D, Piris MA, Ahn N, Imhof A, Caldas C, Jenuwein T, Esteller M. Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer. Nat Genet 2005; 37(4): 391–400 doi: 10.1038/ng1531 pmid:15765097
30	Pfister S, Rea S, Taipale M, Mendrzyk F, Straub B, Ittrich C, Thuerigen O, Sinn HP, Akhtar A, Lichter P. The histone acetyltransferase hMOF is frequently downregulated in primary breast carcinoma and medulloblastoma and constitutes a biomarker for clinical outcome in medulloblastoma. Int J Cancer 2008; 122(6): 1207–1213 doi: 10.1002/ijc.23283 pmid:18058815
31	Patani N, Jiang WG, Newbold RF, Mokbel K. Histone-modifier gene expression profiles are associated with pathological and clinical outcomes in human breast cancer. Anticancer Res 2011; 31(12): 4115–4125 pmid:22199269
32	Liu B, Wei DP, Hu LN, Cui Ling. Expression and clinical significance of hMOF and P53 protein in cervical lesion. J Med West China (Xi Bu Yi Xue) 2011; 23(5): 817–819 (in Chinese)
33	Song JS, Chun SM, Lee JY, Kim DK, Kim YH, Jang SJ. The histone acetyltransferase hMOF is overexpressed in non-small cell lung carcinoma. Korean Journal of Pathology 2011; 45(4): 386–396 doi:10.4132/KoreanJPathol.2011.45.4.386
34	Kruse JP, Gu W. MSL2 promotes Mdm2-independent cytoplasmic localization of p53. J Biol Chem 2009; 284(5): 3250–3263 doi: 10.1074/jbc.M805658200 pmid:19033443
35	Ruthenburg AJ, Li H, Milne TA, Dewell S, McGinty RK, Yuen M, Ueberheide B, Dou Y, Muir TW, Patel DJ, Allis CD. Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactions. Cell 2011; 145(5): 692–706 doi: 10.1016/j.cell.2011.03.053 pmid:21596426
36	Ang YS, Tsai SY, Lee DF, Monk J, Su J, Ratnakumar K, Ding J, Ge Y, Darr H, Chang B, Wang J, Rendl M, Bernstein E, Schaniel C, Lemischka IR. Wdr5 mediates self-renewal and reprogramming via the embryonic stem cell core transcriptional network. Cell 2011; 145(2): 183–197 doi: 10.1016/j.cell.2011.03.003 pmid:21477851
37	Loh YH, Wu Q, Chew JL, Vega VB, Zhang W, Chen X, Bourque G, George J, Leong B, Liu J, Wong KY, Sung KW, Lee CW, Zhao XD, Chiu KP, Lipovich L, Kuznetsov VA, Robson P, Stanton LW, Wei CL, Ruan Y, Lim B, Ng HH. The Oct4 and Nanog transcription network regulates pluripotency in mouse embryonic stem cells. Nat Genet 2006; 38(4): 431–440 doi: 10.1038/ng1760 pmid:16518401
38	Fazzio TG, Huff JT, Panning B. An RNAi screen of chromatin proteins identifies Tip60-p400 as a regulator of embryonic stem cell identity. Cell 2008; 134(1): 162–174 doi: 10.1016/j.cell.2008.05.031 pmid:18614019
39	Lin W, Srajer G, Evrard YA, Phan HM, Furuta Y, Dent SY. Developmental potential of Gcn5(–/–) embryonic stem cells in vivo and in vitro. Dev Dyn 2007; 236(6): 1547–1557 doi: 10.1002/dvdy.21160 pmid:17440986
40	Zhong X, Jin Y. Critical roles of coactivator p300 in mouse embryonic stem cell differentiation and Nanog expression. J Biol Chem 2009; 284(14): 9168–9175 doi: 10.1074/jbc.M805562200 pmid:19150979

[1]	Hai Wang,Qian Zhang,Xiangdong Fang. Transcriptomics and proteomics in stem cell research[J]. Front. Med., 2014, 8(4): 433-444.
[2]	Fung Zhao, Eric W.-F. Lam. Role of the forkhead transcription factor FOXO-FOXM1 axis in cancer and drug resistance[J]. Front Med, 2012, 6(4): 376-380.
[3]	ZHANG Xufeng, YU Liang, LU Yi. Wnt/β-catenin signaling pathway and its role in hepatocellular carcinoma[J]. Front. Med., 2008, 2(3): 216-228.

Viewed

Full text

Abstract

Cited

Shared

Discussed