| First Author | Yu T | Year | 2023 |
| Journal | Cell Rep | Volume | 42 |
| Issue | 10 | Pages | 113231 |
| PubMed ID | 37804507 | Mgi Jnum | J:358034 |
| Mgi Id | MGI:7544792 | Doi | 10.1016/j.celrep.2023.113231 |
| Citation | Yu T, et al. (2023) TRIM11 attenuates Treg cell differentiation by p62-selective autophagic degradation of AIM2. Cell Rep 42(10):113231 |
| abstractText | Ubiquitination is an important protein modification that regulates diverse biological processes, including CD4(+) T cell differentiation and functions. However, the function of most E3 ubiquitin ligases in CD4(+) T cell differentiation and CD4(+) T cell-mediated pathological diseases remains unclear. In this study, we find that tripartite motif-containing motif 11 (TRIM11) specifically negatively regulates regulatory T (Treg) cell differentiation in CD4(+) T cells and promotes autoimmune disease development in an AIM2-dependent manner. Mechanistically, TRIM11 interacts with absent in melanoma 2 (AIM2) and promotes the selective autophagic degradation of AIM2 by inducing AIM2 ubiquitination and binding to p62 in CD4(+) T cells. AIM2 attenuates AKT and FOXO1 phosphorylation, MYC signaling, and glycolysis, thereby promoting the stability of Treg cells during experimental autoimmune encephalomyelitis (EAE). Our findings suggest that TRIM11 serves as a potential target for immunotherapeutic intervention for dysregulated immune responses that lead to autoimmunity and cancers. |
