Journal
CENTRAL EUROPEAN JOURNAL OF IMMUNOLOGY
Volume 38, Issue 1, Pages 15-22Publisher
TERMEDIA PUBLISHING HOUSE LTD
DOI: 10.5114/ceji.2013.34353
Keywords
flow cytometry; pull down; regulator; RING finger protein 166; T cell activation
Categories
Funding
- National Basic Research Program of China (973 Program) [2012CB947600]
- National Natural Science Foundation of China [90919006, 31070676]
- Trans-Century Training Program Foundation for the Talents by the Ministry of Education of China [NCET-07-0580]
- Spring Sunshine Program by the Ministry of Education of China [Z2009-1-61003]
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RING (really interesting new gene) finger protein 166, or RNF166, belongs to a C3HC4 ubiquitin ligases subfamily, which include four related proteins containing a conserved C3HC4 (Cys3-His-Cys4) RING finger domain. RNF125, one member of the subfamily, has been identified as a regulator of T cell activation, but the potential roles of another member RNF166 remains poorly understood. Here we reported that RNF166 is involved in regulation of T cell activation. Flow cytometry (FCM) data showed that overexpression of RNF166 in primary T cells and Jurkat T cells induced over 2-fold increase of CD69, a T-cell activation marker, suggesting that RNF166 is a positive-regulator of T cell activation. Furthermore, pull-down assays showed that RNF166 can bind with both Lys(48)-linked polyubiquitin and Lys(63)-linked polyubiquitin, indicating that RNF166 may play regulating roles in T cell activation by self-degradation via ubiquitin-proteasome pathway and/or cross-talk with certain signaling pathways via non-proteasome-dependent pathways. In conclusion, our work reveals that RNF166 is a potential positive-regulator of T cell activation and these findings provide a novel insight into understanding the functions of RNF166 in the positive regulation of immune responses.
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