组蛋白去甲基化酶LSD1及其生物学功能

doi:10.3724/SP.J.1005.2010.00331

[an error occurred while processing this directive]

HEREDITAS ›› 2010, Vol. 32 ›› Issue (4): 331-338.doi: 10.3724/SP.J.1005.2010.00331

• en • Previous Articles Next Articles

Histone demethylase LSD1 and its biological functions

SHAO Gen-Bao, HUANG Xiao-Jia, GONG Ai-Hua, ZHANG Zhi-Jian, LU Rong-Zhu, SANG Jian-Rong

Institute of Basic Medical Science, School of Medicine, Jiangsu University, Zhenjiang 212013, China

Received:2009-08-16 Revised:2009-10-20 Online:2010-04-20 Published:2010-04-15
Contact: SHAO Gen-Bao E-mail:genbaoshao@163.com

Abstract

Abstract: Discovery of histone lysine specific demethylase 1 (LSD1) indicates that even histone methylation is reversible. Structural analysis shows that LSD1 is a flavin-dependent amine oxidase, which is able to catalyze the specific removal of methyl groups from mono- and dimethylated Lys4 and Lys9 of histone H3. Functional studies demonstrate that LSD1 regulates activation and inhibition of gene transcription in the nucleus, which is known as the innermost gene switch of cells. LSD1 plays important roles in embryonic development and tumorigenesis. Here, we review recent insights into the structure and chemical mechanism of LSD1, and its regulatory roles in development and cancer.

Key words: gene transcriptional regulation, cancer suppression, embryonic development, LSD1, histone demethylase

SHAO Gen-Bao, HUANG Xiao-Jia, GONG Ai-Hua, ZHANG Zhi-Jian, LIU Rong-Zhu, SANG Jian-Rong. Histone demethylase LSD1 and its biological functions[J]. HEREDITAS, 2010, 32(4): 331-338.

References

[1] Kornberg RD, Lorch Y. Twenty-five years of the nu-cleosome, fundamental particle of the eukaryote chromo-some. Cell, 1999, 98(3): 285−294. [2] Kouzarides T. Chromatin modifications and their function. Cell, 2007, 128(4): 693−705. [3] Shahbazian MD, Grunstein M. Functions of site-specific histone acetylation and deacetylation. Annu Rev Biochem, 2007, 76(2): 75−100. [4] Marmorstein R, Trievel RC. Histone modifying enzymes: structures, mechanisms, and specificities. Biochim Biophys Acta, 2009, 1789(1): 58−68. [5] Zhang Y. Transcriptional regulation by histone ubiquitination and deubiquitination. Genes Dev, 2003, 17(22): 2733−2740. [6] Shi Y, Lan F, Matson C, Mulligan P, Whetstine JR, Cole PA, Casero RA, Shi Y. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell, 2004, 119(7): 941−953. [7] Chen Y, Yang Y, Wang F, Wan K, Yamane K, Zhang Y, Lei M. Crystal structure of human histone lysine-specific de-methylase 1 (LSD1). Proc Natl Acad Sci USA, 2006, 103(38): 13956−13961. [8] Anand R, Marmorstein R. Structure and mechanism of ly-sine-specific demethylase enzymes. J Biol Chem, 2007, 282(49): 35425−35429. [9] 阮建彬, 臧建业. 组蛋白去甲基化酶LSD1 的结构和功能研究进展. 中国科学技术大学学报, 2008, 38(8): 930−940. [10] Lee MG, Wynder C, Bochar DA, Hakimi MA, Cooch N, Shiekhattar R. Functional interplay between histone de-methylase and deacetylase enzymes. Mol Cell Biol, 2006, 26(17): 6395−6402. [11] Yang M, Gocke CB, Luo X, Borek D, Tomchick DR, Machius M, Otwinowski Z, Yu H. Structural basis for CoREST dependent demethylation of nucleosomes by the human LSD1 histone demethylase. Mol Cell, 2006, 23(3): 377−387. [12] Lan F, Nottke AC, Shi Y. Mechanisms involved in the regulation of histone lysine demethylases. Curr Opin Cell Biol, 2008, 20(3): 316−325. [13] Nottke A, Colaiacovo MP, Shi Y. Developmental roles of the histone lysine demethylases. Development, 2009, 136(6): 879−889. [14] 高文龙, 刘红林. DOT1—— 一类新的组蛋白赖氨酸甲基转移酶. 遗传, 2007, 29(12): 1449−1454. [15] Karytinos A, Forneris F, Profumo A, Ciossani G, Battaglioli E, Binda C, Mattevi A. A novel mammalian flavin-dependent histone demethylase. J Biol Chem, 2009, 284(26): 17775−17782. [16] Rudolph T, Yonezawa M, Lein S, Heidrich K, Kubicek S, Schafer C, Phalke S, Walther M, Schmidt A, Jenuwein T, Reuter G. Heterochromatin formation in Drosophila is ini-tiated through active removal of H3K4 methylation by the LSD1 homolog SU(VAR)3-3. Mol Cell, 2007, 26(1): 103−115. [17] Eimer S, Lakowski B, Donhauser R, Baumeister R. Loss of spr-5 bypasses the requirement for the C. elegans pre-senilin sel-12 by derepressing hop-1. EMBO J, 2002, 21(21): 5787−5796. [18] Huang J, Sengupta R, Espejo AB, Lee MG, Dorsey JA, Richter M, Opravil S, Shiekhattar R, Bedford MT, Jenuwein T, Berger SL. p53 is regulated by the lysine de-methylase LSD1. Nature, 2007, 449(7158): 105−108. [19] Nicholson TB, Chen T. LSD1 demethylates histone and non-histone proteins. Epigenetics, 2009, 4(3): 129−132. [20] Jiang D, Yang W, He Y, Amasino RM. Arabidopsis rela-tives of the human lysine-specific Demethylase1 repress the expression of FWA and FLOWERING LOCUS C and thus promote the floral transition. Plant Cell, 2007, 19(10): 2975−2987. [21] Wang L, Pei Z, Tian Y, He C. OsLSD1, a rice zinc finger protein, regulates programmed cell death and callus dif-ferentiation. Mol Plant Microbe Interact, 2005, 18(5): 375−384. [22] Tsukada Y, Fang J, Erdjument-Bromage H, Warren ME, Borchers CH,Tempst P, Zhang Y. Histone demethylation by a family of JmjC domain-containing proteins. Nature, 2006, 439(7078): 811−816. [23] Yamane K, Toumazou C, Tsukada Y, Erdjument-Bromage H, Tempst P, Wong J, Zhang Y. JHDM2A, a JmjC-con

Metrics

Comments

www.chinagene.cn
备案号：京ICP备09063187号

Histone demethylase LSD1 and its biological functions

PDF (PC)

Knowledge

Abstract

Cite this article

share this article

References

Related Articles 8

Recommended Articles

Metrics

Comments

[1]	Guangwei Hu, Zhenzhen Zhang, Huan Gao. Progress on the left-right asymmetry patterning in amphioxus [J]. Hereditas(Beijing), 2021, 43(2): 134-141.
[2]	Chunyou Ning,Mengnan He,Qianzi Tang,Qing Zhu,Mingzhou Li,Diyan Li. Advances in mammalian three-dimensional genome by using Hi-C technology approach [J]. Hereditas(Beijing), 2019, 41(3): 215-233.
[3]	Mei Fu, Kehui Xu, Wenming Xu. Research advances of Dicer in regulating reproductive function [J]. HEREDITAS(Beijing), 2016, 38(7): 612-622.
[4]	Yuanyuan Li, Lei Guo, Shengsheng Lu, Zhiming Han. Role of parathyroid hormone-like hormone during embryonic development [J]. HEREDITAS(Beijing), 2014, 36(9): 871-878.
[5]	Shaoqin Ge, Zhenghui Zhao, Xueqian Zhang, Yuan Hao. Epigenetic modifications in human spermatozoon and its potential role in embryonic development [J]. HEREDITAS(Beijing), 2014, 36(5): 439-446.
[6]	QIN Wei, HU Zhan-Ying, TONG Jun-Wei, MENG Jie, YOU Xue-Fu, ZHANG Jing-Pu. Toxic effects of trimethadione on zebrafish early development [J]. HEREDITAS, 2012, 34(9): 1165-1173.
[7]	HE Chong-Bo, ZHU Bao, LIU Wei-Dong, BAO Xiang-Bo, LI Yun-Feng, SHAN Zhong-Guo, LI Hong-Jun. Cloning and expression analysis of lipopolysaccharide-induced TNF-a(LITAF) of Japanese scallop (Mizuhopecten yessoensis) [J]. HEREDITAS, 2012, 34(6): 736-741.
[8]	MA Tie-Fu, YANG Dong, HE Fu-Chu, JIANG Ying. Review for the regulatory functions of KRAB zinc finger proteins in embryonic development and tumorgenesis of higher vertebrates [J]. HEREDITAS, 2010, 32(5): 431-436.