Regulation of immune responses by E3 ubiquitin ligase Cbl-b

被引:69
作者
Tang, Rong [1 ]
Langdon, Wallace Y. [2 ]
Zhang, Jian [3 ]
机构
[1] Cent South Univ, Dept Nephrol, Xiangya Hosp, Changsha, Hunan, Peoples R China
[2] Univ Western Australia, Sch Biol Sci, Perth, WA, Australia
[3] Univ Iowa, Dept Pathol, Iowa City, IA 52242 USA
基金
美国国家卫生研究院;
关键词
Cbl-b; Ubiquitination; Innate and adaptive immune responses; T cell tolerance; Immune-related disorders; T-CELL DEVELOPMENT; NEGATIVE REGULATION; C-CBL; K33-LINKED POLYUBIQUITINATION; ACTIVATION THRESHOLD; CUTTING EDGE; BINDING-SITE; UBA DOMAINS; RING-TYPE; PROTEIN;
D O I
10.1016/j.cellimm.2018.11.002
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Casitas B lymphoma-b (Cbl-b), a RING finger E3 ubiquitin ligase, has been identified as a critical regulator of adaptive immune responses. Cbl-b is essential for establishing the threshold for T cell activation and regulating peripheral T cell tolerance through various mechanisms. Intriguingly, recent studies indicate that Cbl-b also modulates innate immune responses, and plays a key role in host defense to pathogens and anti-tumor immunity. These studies suggest that targeting Cbl-b may represent a potential therapeutic strategy for the management of human immune-related disorders such as autoimmune diseases, infections, tumors, and allergic airway inflammation. In this review, we summarize the latest developments regarding the roles of Cbl-b in innate and adaptive immunity, and immune-mediated diseases.
引用
收藏
页数:9
相关论文
共 103 条
[1]  
Acharya D, 2017, J VIROL, V91, DOI [10.1128/JVI.01529-16, 10.1128/jvi.01529-16]
[2]   CD28-mediated co-stimulation: A quantitative support for TCR signalling [J].
Acuto, O ;
Michel, F .
NATURE REVIEWS IMMUNOLOGY, 2003, 3 (12) :939-951
[3]   Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b [J].
Bachmaier, K ;
Krawczyk, C ;
Kozieradzki, I ;
Kong, YY ;
Sasaki, T ;
Oliveira-dos-Santos, A ;
Mariathasan, S ;
Bouchard, D ;
Wakeham, A ;
Itie, A ;
Le, J ;
Ohashi, PS ;
Sarosi, I ;
Nishina, H ;
Lipkowitz, S ;
Penninger, JM .
NATURE, 2000, 403 (6766) :211-216
[4]   E3 ubiquitin ligase Cblb regulates the acute inflammatory response underlying lung injury [J].
Bachmaier, Kurt ;
Toya, Sophie ;
Gao, Xiaopei ;
Triantafillou, Thomas ;
Garrean, Sean ;
Park, Gye Young ;
Frey, Randall S. ;
Vogel, Stephen ;
Minshall, Richard ;
Christman, John W. ;
Tiruppathi, Chinnaswamy ;
Malik, Asrar B. .
NATURE MEDICINE, 2007, 13 (08) :920-926
[5]   Ubiquitylation in innate and adaptive immunity [J].
Bhoj, Vijay G. ;
Chen, Zhijian J. .
NATURE, 2009, 458 (7237) :430-437
[6]   Ablation of Cbl-b provides protection against transplanted and spontaneous tumors [J].
Chiang, Jeffrey Y. ;
Jang, Ihn Kyung ;
Hodes, Richard ;
Gu, Hua .
JOURNAL OF CLINICAL INVESTIGATION, 2007, 117 (04) :1029-1036
[7]   Cbl-b regulates the CD28 dependence of T-cell activation [J].
Chiang, YPJ ;
Kole, HK ;
Brown, K ;
Naramura, M ;
Fukuhara, S ;
Hu, RJ ;
Jang, IK ;
Gutkind, JS ;
Shevach, E ;
Gu, H .
NATURE, 2000, 403 (6766) :216-220
[8]   Cbl-b interacts with ubiquitinated proteins; differential functions of the UBA domains of c-Cbl and Cbl-b [J].
Davies, GC ;
Ettenberg, SA ;
Coats, AO ;
Mussante, M ;
Ravichandran, S ;
Collins, J ;
Nau, MM ;
Lipkowitz, S .
ONCOGENE, 2004, 23 (42) :7104-7115
[9]   Essentiality of a non-RING element in priming donor ubiquitin for catalysis by a monomeric E3 [J].
Dou, Hao ;
Buetow, Lori ;
Sibbet, Gary J. ;
Cameron, Kenneth ;
Huang, Danny T. .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2013, 20 (08) :982-+
[10]   RING-Between-RING E3 Ligases: Emerging Themes amid the Variations [J].
Dove, Katja K. ;
Klevit, Rachel E. .
JOURNAL OF MOLECULAR BIOLOGY, 2017, 429 (22) :3363-3375