组蛋白H3.3导致肿瘤发生的研究进展

陈曦; 吴刚; 吴登龙

doi:10.13201/j.issn.1001-1420.2019.09.015

组蛋白H3.3导致肿瘤发生的研究进展

- 同济大学附属同济医院泌尿外科(上海, 200065)
基金项目:
国家自然科学基金（编号81672526）

详细信息

通讯作者: 吴登龙,E-mail:wudenglong2013@126.com

中图分类号: R329

收稿日期: 2018-09-16

Current research progress of histone H3.3 induced tumorigenesis

- Department of Urology, Tongji Hospital of Tongji University, Shanghai, 200065, China

More Information

Corresponding author: WU Denglong, E-mail: wudenglong2013@126.com

Received Date: 16 September 2018

摘要

摘要: 组蛋白是真核生物染色体的重要组成成分，在真核生物细胞有丝分裂、减数分裂及胚胎发育过程中组蛋白均起着重要的作用。不同类型的组蛋白有着不同的特异结构并参与调节染色体的结构，从而保证了基因组DNA在整个细胞分裂周期中的精准复制并维持染色体结构的稳定。组蛋白H3.3作为组蛋白变异体的重要一员，其在基因转录、DNA损伤修复及维持染色体的正常结构中均发挥着独特且重要作用。因此，当组蛋白H3.3发生突变之后会导致包括肿瘤在内多种疾病的发生。本文就目前对于组蛋白H3.3导致肿瘤发生的研究进展作一综述。
- 组蛋白H3.3 /
- 染色体 /
- 肿瘤
Abstract: Histones are the main protein components of eukaryotic chromatin. Histone plays an important role in mitosis, meiosis and embryonic development process. Different histones have many special different structures so they can modulate chromatin structure, ensuring the precise operation of cellular processes associated with genomic DNA and maintain the stability of chromatin. H3.3, an important H3 variant, plays an essential and specific role in gene transcription, DNA repair and maintaining genome integrity. So when histone H3.3 mutation occurs, it will lead to the occurrence of many diseases, including tumors. Here, we review the current research progress of histone H3.3 induced tumorigenesis.
- histone H3.3 /
- chromosome /
- tumor

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参考文献(31)

[1]	Kirmizis A, Santos-Rosa H, Penkett C J, et al.Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation[J].Nature, 2007, 449(7164):928-932.
[2]	Henikoff S, Ahmad K.Assembly of variant histones into chromatin[J].Annu Rev Cell Dev Biol, 2005, 21:133-153.
[3]	Marzluff W F, Duronio R J.Histone mRNA expression:multiple levels of cell cycle regulation and important developmental consequences[J].Curr Opin Cell Biol, 2002, 14(6):692-699.
[4]	Szenker E, Ray-Gallet D, Almouzni G.The double face of the histone variant H3.3[J].Cell Res, 2011, 21(3):421-434.
[5]	Hamiche A, Shuaib M.Chaperoning the histone H3 family[J].Biochim Biophys Acta, 2013, 1819(3-4):230-237.
[6]	Frank D, Doenecke D, Albig W.Differential expression of human replacement and cell cycle dependent H3 histone genes[J].Gene, 2003, 312:135-143.
[7]	Filipescu D, Szenker E, Almouzni G.Developmental roles of histone H3 variants and their chaperones[J].Trends Genet, 2013, 29(11):630-640.
[8]	Ahmad K, Henikoff S.The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly[J].Mol Cell, 2002, 9(6):1191-1200.
[9]	Chen P, Zhao J, Wang Y, et al.H3.3 actively marks enhancers and primes gene transcription via opening higher-ordered chromatin[J].Genes Dev, 2013, 27:2109-2124.
[10]	Banaszynski L A, Wen D, Dewell S, et al.Hira-dependent histone H3.3 deposition facilitates PRC2 recruitment at developmental loci in ES cells[J].Cell, 2013, 155(1):107-120.
[11]	Jin C, Zang C, Wei G, et al.H3.3/H2A.Z double variant-containing nucleosomes mark ‘nucleosome-free regions’ of active promoters and other regulatory regions[J].Nat Genet, 2009, 41(8):941-945.
[12]	Straub M, Hautmann R E.Developments in stone prevention[J].Curr Opin Urol, 2005, 15(2):119-126.
[13]	Goldberg A D, Banaszynski L A, Noh K M, et al.Distinct factors control histone variant H3.3 localization at specific genomic regions[J].Cell, 2010, 140(5):678-691.
[14]	Wong L H, McGhie J D, Sim M, et al.ATRX interacts with H3.3 in maintaining telomere structural integrity in pluripotent embryonic stem cells[J].Genome Res, 2010, 20(3):351-360.
[15]	Elsässer S J, Noh K M, Diaz N, et al.Histone H3.3 is required for endogenous retroviral element silencing in embryonic stem cells[J].Nature, 2015, 522(7555):240-244.
[16]	Sturm D, Witt H, Hovestadt V, et al.Hotspot mutations in H3F3Aand IDH1define distinct epigenetic and biological subgroups of glioblastoma[J].Cancer Cell, 2012, 22(4):425-437.
[17]	Behjati S, Tarpey P S, Presneau N, et al.Distinct H3F3A and H3F3B driver mutations define chondroblastoma and giant cell tumor of bone[J].Nat Genet, 2013, 45(12):1479-1482.
[18]	Yuen B T, Knoepfler P S.Histone H3.3 mutations:a variant path to cancer[J].Cancer Cell, 2013, 24(5):567-574.
[19]	Zhang R, Han J, Daniels D, et al.Detecting the H3F3 Amutant allele found in high-grade pediatric glioma by real-time PCR[J].J Neurooncol, 2016, 126(1):27-36.
[20]	Bender S, Tang Y, Lindroth A M, et al.Reduced H3K27me3 and DNA hypomethylation are major drivers of gene expression in K27M mutant pediatric highgrade gliomas[J].Cancer Cell, 2013, 24(5):660-672.
[21]	Schwartzentruber J, Korshunov A, Liu X Y, et al.Driver mutations in histone H3.3 and chromatin remodelling genes in paediatric glioblastoma[J].Nature, 2012, 482(7384):226-231.
[22]	Cordero F J, Huang Z, Grenier C, et al.Histone H3.3K27M Represses p16 to Accelerate Gliomagenesis in a Murine Model of DIPG[J].Mol Cancer Res, 2017, 15(9):1243-1254.
[23]	Presneau N, Baumhoer D, Behjati S, et al.Diagnostic value of H3F3A mutations in giant cell tumour of bone compared to osteoclast-rich mimics[J].J Pathol Clin Res, 2015, 1(2):113-123.
[24]	Bjerke L, Mackay A, Nandhabalan M, et al.Histone H3.3.mutations drive pediatric glioblastoma through upregulation of MYCN[J].Cancer Discov, 2013, 3(5):512-519.
[25]	Lewis P W, Müller M M, Koletsky M S, et al.Inhibition of PRC2 activity by again-of-function H3 mutation found in pediatric glioblastoma[J].Science, 2013, 340(6134):857-861.
[26]	Jha P, Pia Patric I R, Shukla S, et al.Genome-wide methylation profiling identifies an essential role of reactive oxygen species in pediatric glioblastoma multiforme and validates a methylome specific for H3 histone family 3A with absence of G-CIMP/isocitrate dehydrogenase 1mutation[J].Neuro Oncol, 2014, 16(12):1607-1617.
[27]	Fontebasso A M, Gayden T, Nikbakht H.et al.Epigenetic dysregulation:a novel pathway of oncogenesis in pediatric brain tumors[J].Acta Neuropathol, 2014, 128(5):615-627.
[28]	Wagner E J, Carpenter P B.Understanding the language of Lys36 methylation at histone H3[J].Nat Rev Mol Cell Biol, 2012, 13(2):115-126.
[29]	Wen H, Li Y, Xi Y, et al.ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppression[J].Nature, 2014, 508(7495):263-268.
[30]	Koelsche C, Schrimpf D, Tharun L, et al.Histone 3.3hotspot mutations in conventional osteosarcomas:a comprehensive clinical and molecular characterization of six H3F3A mutated cases[J].Clin Sarcoma Res, 2017, 7:9.
[31]	Benitez J A, Ma J, D'Antonio M, et al.PTEN regulates glioblastoma oncogenesis through chromatin-associated complexes of DAXX and histone H3.3[J].Nat Commun, 2017, 8:15223.