Ubiquitin-Dependent Regulation of Treg Function and Plasticity

被引:2
|
作者
Dong, Yi [1 ]
Pan, Fan [2 ]
机构
[1] Johns Hopkins Univ, Sch Med, Dept Cell Biol, Baltimore, MD USA
[2] Chinese Acad Sci, Shenzhen Inst Adv Technol, Ctr Canc Immunol Res, Shenzhen, Guangdong, Peoples R China
来源
T REGULATORY CELLS IN HUMAN HEALTH AND DISEASES | 2021年 / 1278卷
关键词
Treg; Ubiquitin; Posttranslational regulation; Foxp3; T-CELL DEVELOPMENT; TRANSCRIPTION FACTOR FOXP3; DE-NOVO DIFFERENTIATION; TGF-BETA; AUTOIMMUNE-DISEASE; SELF-TOLERANCE; CUTTING EDGE; CBL-B; LINEAR UBIQUITINATION; SUPPRESSIVE FUNCTION;
D O I
10.1007/978-981-15-6407-9_4
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
As an indispensable part of peripheral tolerance, regulatory T (Treg) cells play an important role in immune homeostasis by suppressing other immune cells. Behind this function is a complex network of transcription factors and signaling cascades that regulates the function and plasticity of regulatory T cells. Among these, Forkhead box P3 (Foxp3) is considered as the master transcription factor, and its stability will influence the function and viability of Treg cells. Because of this, understanding the mechanisms that regulate Foxp3 and its co-regulators will provide more understanding to Treg cells and uncover more targets to manipulate Treg cells in treating autoimmune diseases, organ transplantation, and tumor. Interestingly, several recent studies show that ubiquitin-dependent pathways are important regulators of Foxp3, which suggest both great scientific and therapeutic values. In this chapter, we cover emerging evidence of ubiquitin-dependent, posttranslational regulation of Treg function and plasticity.
引用
收藏
页码:63 / 80
页数:18
相关论文
共 50 条
  • [31] Emerging regulatory mechanisms in ubiquitin-dependent cell cycle control
    Mocciaro, Annamaria
    Rape, Michael
    JOURNAL OF CELL SCIENCE, 2012, 125 (02) : 255 - 263
  • [32] Calorie restriction, stress and the ubiquitin-dependent pathway in mouse livers
    Scrofano, MM
    Shang, F
    Nowell, TR
    Gong, X
    Smith, DE
    Kelliher, M
    Dunning, J
    Mura, CV
    Taylor, A
    MECHANISMS OF AGEING AND DEVELOPMENT, 1998, 105 (03) : 273 - 290
  • [33] Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation
    Kriegenburg, Franziska
    Ellgaard, Lars
    Hartmann-Petersen, Rasmus
    FEBS JOURNAL, 2012, 279 (04) : 532 - 542
  • [34] Intracellular proteinases of invertebrates: Calcium-dependent and proteasome/ubiquitin-dependent systems
    Mykles, DL
    INTERNATIONAL REVIEW OF CYTOLOGY - A SURVEY OF CELL BIOLOGY, VOL 184, 1998, 184 : 157 - 289
  • [35] E6AP Ubiquitin Ligase Mediates Ubiquitin-Dependent Degradation of Peroxiredoxin 1
    Nasu, Junichi
    Murakami, Kyoko
    Miyagawa, Shoji
    Yamashita, Ryosuke
    Ichimura, Tohru
    Wakita, Takaji
    Hotta, Hak
    Miyamura, Tatsuo
    Suzuki, Tetsuro
    Satoh, Tazuko
    Shoji, Ikuo
    JOURNAL OF CELLULAR BIOCHEMISTRY, 2010, 111 (03) : 676 - 685
  • [36] Acquisition of glutamine synthetase expression in human hepatocarcinogenesis -: Relation to disease recurrence and possible regulation by ubiquitin-dependent proteolysis
    Osada, T
    Sakamoto, M
    Nagawa, H
    Yamamoto, J
    Matsuno, Y
    Iwamatsu, A
    Muto, T
    Hirohashi, S
    CANCER, 1999, 85 (04) : 819 - 831
  • [37] A small ubiquitin binding domain inhibits ubiquitin-dependent protein recruitment to DNA repair foci
    Helchowski, Corey M.
    Skow, Laura F.
    Roberts, Katelyn H.
    Chute, Colleen L.
    Canman, Christine E.
    CELL CYCLE, 2013, 12 (24) : 3749 - 3758
  • [38] Ubiquitin-dependent pathway is up-regulated in differentiating lens cells
    Shang, F
    Gong, X
    McAvoy, JW
    Chamberlain, C
    Nowell, TR
    Taylor, A
    EXPERIMENTAL EYE RESEARCH, 1999, 68 (02) : 179 - 192
  • [39] Celastrol induces ubiquitin-dependent degradation of mTOR in breast cancer cells
    Li, Xiaoli
    Zhu, Guangbei
    Yao, Xintong
    Wang, Ning
    Hu, Ronghui
    Kong, Qingxin
    Zhou, Duanfang
    Long, Liangyuan
    Cai, Jiali
    Zhou, Weiying
    ONCOTARGETS AND THERAPY, 2018, 11 : 8977 - 8985
  • [40] NGF augments the autophosphorylation of Ret via inhibition of ubiquitin-dependent degradation
    Pierchala, Brian A.
    Tsui, Cynthia C.
    Milbrandt, Jeffrey
    Johnson, Eugene M.
    JOURNAL OF NEUROCHEMISTRY, 2007, 100 (05) : 1169 - 1176