标题:Role of citrullination modification catalyzed by peptidylarginine deiminase 4 in gene transcriptional regulation
作者:Zhai, Qiaoli; Wang, Lianqing; Zhao, Peiqing; Li, Tao
作者机构:[Zhai Qiaoli] Center of Translational Medicine, Central Hospital of Zibo, Shandong University, Zibo, Shandong 255036, China.;[Wang Lianqing] Center of 更多
通讯作者:Li, T(zbszxyyky@163.com)
通讯作者地址:[Li, T]Shandong Univ, Cent Hosp Zibo, Ctr Translat Med, Zibo 255036, Peoples R China.
来源:生物化学与生物物理学报
出版年:2017
卷:49
期:7
页码:567-572
DOI:10.1093/abbs/gmx042
关键词:peptidylarginine deiminase 4; citrullination; post-translational; modification; transcriptional regulation
摘要:Peptidylarginine deiminase 4 (PADI4), a new histone modification enzyme, which converts both arginine and monomethyl-arginine to citrulline, has gained massive attention in recent years as a potential regulator of gene transcription. Recent studies have shown that arginine residues R2, R8, R17, and R26 in the H3 tail and R3 in the H4 tail can be deiminated by PADI4. This kind of histone post-translational modification has the potential to antagonize histone methylation and coordinate with histone deacetylation to regulate gene transcription. PADI4 also deiminates non-histone proteins, such as p300, NPM1, ING4, RPS2, and DNMT3A. PADI4 has been shown to involve in cell apoptosis and differentiation. Moreover, PADI4 can interact with tumor suppressor p53 and regulate the transcriptional activity of p53. Dysregulation of PADI4 is implicated in a variety of diseases, including rheumatoid arthritis, tumor development, and multiple sclerosis. A wide variety of PADI4 inhibitors have been identified. Further understanding of PADI4 functions may lead to novel diagnostic and therapeutic approaches in these diseases. This review summarizes the recent progress in the study of the regulation mechanism of PADI4 on gene transcription and the major physiological functions of PADI4 in human diseases.
收录类别:CSCD;SCOPUS;SCIE
Scopus被引频次:1
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85023163970&doi=10.1093%2fabbs%2fgmx042&partnerID=40&md5=680b1b31dda9709792b868e187476553
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