HBO1, a MYSTerious KAT and Its Links to Cancer

Overview

Journal Biochim Biophys Acta Gene Regul Mech

Publisher Elsevier

Specialties Biochemistry
Biophysics
Genetics
Molecular Biology

Date 2024 Jun 8

PMID 38851533

Authors

Akihiko Yokoyama

Hiroyuki Niida

Tatiana G Kutateladze

Jacques Cote

Affiliations

Soon will be listed here.

Abstract

The histone acetyltransferase HBO1, also known as KAT7, is a major chromatin modifying enzyme responsible for H3 and H4 acetylation. It is found within two distinct tetrameric complexes, the JADE subunit-containing complex and BRPF subunit-containing complex. The HBO1-JADE complex acetylates lysine 5, 8 and 12 of histone H4, and the HBO1-BRPF complex acetylates lysine 14 of histone H3. HBO1 regulates gene transcription, DNA replication, DNA damage repair, and centromere function. It is involved in diverse signaling pathways and plays crucial roles in development and stem cell biology. Recent work has established a strong relationship of HBO1 with the histone methyltransferase MLL/KMT2A in acute myeloid leukemia. Here, we discuss functional and pathological links of HBO1 to cancer, highlighting the underlying mechanisms that may pave the way to the development of novel anti-cancer therapies.

References

Yokoyama A, Cleary M . Menin critically links MLL proteins with LEDGF on cancer-associated target genes. Cancer Cell. 2008; 14(1):36-46. PMC: 2692591. DOI: 10.1016/j.ccr.2008.05.003. View

Annunziato A, Hansen J . Role of histone acetylation in the assembly and modulation of chromatin structures. Gene Expr. 2000; 9(1-2):37-61. PMC: 5964959. DOI: 10.3727/000000001783992687. View

Gough S, Slape C, Aplan P . NUP98 gene fusions and hematopoietic malignancies: common themes and new biologic insights. Blood. 2011; 118(24):6247-57. PMC: 3236115. DOI: 10.1182/blood-2011-07-328880. View

Yang X . MOZ and MORF acetyltransferases: Molecular interaction, animal development and human disease. Biochim Biophys Acta. 2015; 1853(8):1818-26. DOI: 10.1016/j.bbamcr.2015.04.014. View

Viita T, Cote J . The MOZ-BRPF1 acetyltransferase complex in epigenetic crosstalk linked to gene regulation, development, and human diseases. Front Cell Dev Biol. 2023; 10:1115903. PMC: 9873972. DOI: 10.3389/fcell.2022.1115903. View

Zentner G, Henikoff S . Regulation of nucleosome dynamics by histone modifications. Nat Struct Mol Biol. 2013; 20(3):259-66. DOI: 10.1038/nsmb.2470. View

Lan R, Wang Q . Deciphering structure, function and mechanism of lysine acetyltransferase HBO1 in protein acetylation, transcription regulation, DNA replication and its oncogenic properties in cancer. Cell Mol Life Sci. 2019; 77(4):637-649. PMC: 11104888. DOI: 10.1007/s00018-019-03296-x. View

Barman S, Roy A, Padhan J, Sudhamalla B . Molecular Insights into the Recognition of Acetylated Histone Modifications by the BRPF2 Bromodomain. Biochemistry. 2022; 61(17):1774-1789. DOI: 10.1021/acs.biochem.2c00297. View

Wang W, Zheng Y, Sun S, Li W, Song M, Ji Q . A genome-wide CRISPR-based screen identifies as a driver of cellular senescence. Sci Transl Med. 2021; 13(575). DOI: 10.1126/scitranslmed.abd2655. View

10.

Li L, Liang Y, Kang L, Liu Y, Gao S, Chen S . Transcriptional Regulation of the Warburg Effect in Cancer by SIX1. Cancer Cell. 2018; 33(3):368-385.e7. DOI: 10.1016/j.ccell.2018.01.010. View

11.

Ohzeki J, Shono N, Otake K, Martins N, Kugou K, Kimura H . KAT7/HBO1/MYST2 Regulates CENP-A Chromatin Assembly by Antagonizing Suv39h1-Mediated Centromere Inactivation. Dev Cell. 2016; 37(5):413-27. PMC: 4906249. DOI: 10.1016/j.devcel.2016.05.006. View

12.

Huntly B, Shigematsu H, Deguchi K, Lee B, Mizuno S, Duclos N . MOZ-TIF2, but not BCR-ABL, confers properties of leukemic stem cells to committed murine hematopoietic progenitors. Cancer Cell. 2004; 6(6):587-96. DOI: 10.1016/j.ccr.2004.10.015. View

13.

Xiao Y, Li W, Yang H, Pan L, Zhang L, Lu L . HBO1 is a versatile histone acyltransferase critical for promoter histone acylations. Nucleic Acids Res. 2021; 49(14):8037-8059. PMC: 8661427. DOI: 10.1093/nar/gkab607. View

14.

Yu B, Hess J, Horning S, Brown G, Korsmeyer S . Altered Hox expression and segmental identity in Mll-mutant mice. Nature. 1995; 378(6556):505-8. DOI: 10.1038/378505a0. View

15.

Niida H, Matsunuma R, Horiguchi R, Uchida C, Nakazawa Y, Motegi A . Phosphorylated HBO1 at UV irradiated sites is essential for nucleotide excision repair. Nat Commun. 2017; 8:16102. PMC: 5520108. DOI: 10.1038/ncomms16102. View

16.

Ayton P, Cleary M . Transformation of myeloid progenitors by MLL oncoproteins is dependent on Hoxa7 and Hoxa9. Genes Dev. 2003; 17(18):2298-307. PMC: 196466. DOI: 10.1101/gad.1111603. View

17.

Clouaire T, Rocher V, Lashgari A, Arnould C, Aguirrebengoa M, Biernacka A . Comprehensive Mapping of Histone Modifications at DNA Double-Strand Breaks Deciphers Repair Pathway Chromatin Signatures. Mol Cell. 2018; 72(2):250-262.e6. PMC: 6202423. DOI: 10.1016/j.molcel.2018.08.020. View

18.

Chen T, Hao H, Zhang Y, Chen X, Zhao H, Yang R . HBO1 induces histone acetylation and is important for non-small cell lung cancer cell growth. Int J Biol Sci. 2022; 18(8):3313-3323. PMC: 9134900. DOI: 10.7150/ijbs.72526. View

19.

Voss A, Thomas T . MYST family histone acetyltransferases take center stage in stem cells and development. Bioessays. 2009; 31(10):1050-61. DOI: 10.1002/bies.200900051. View

20.

Jacquet K, Fradet-Turcotte A, Avvakumov N, Lambert J, Roques C, Pandita R . The TIP60 Complex Regulates Bivalent Chromatin Recognition by 53BP1 through Direct H4K20me Binding and H2AK15 Acetylation. Mol Cell. 2016; 62(3):409-421. PMC: 4887106. DOI: 10.1016/j.molcel.2016.03.031. View