Researchers from the Shanghai Academy of Life Sciences, Chinese Academy of Sciences and the Johns Hopkins University School of Medicine confirmed that ubiquitin ligase Stub1 negatively regulates the inhibitory activity of regulatory T (Treg) cells by promoting the degradation of the transcription factor Foxp3. The research paper was published in the "Immunity" magazine on August 22. Researcher Bin Li of the Shanghai Academy of Life Sciences of the Chinese Academy of Sciences and Dr. Fan Pan of the Johns Hopkins University School of Medicine are co-corresponding authors of this paper. The current research focus of Li Bin's group is a subset of T cells with immunoregulatory functions, namely CD4 + CD25 + FOXP3 + regulatory T cells in major human viral infectious diseases including AIDS, hepatitis B and C viral hepatitis Physiological function and its regulating mechanism. Treg is a special subpopulation of CD4 + cells with low proliferation capacity and ability to suppress immune response. It plays an important role in immunopathology, graft tolerance, preventing autoimmune cell responses and maintaining the body's immune balance. Treg cells have regulatory functions both in vivo and in vivo. The lack or inhibition of Treg cells can lead to various autoimmune diseases such as rheumatoid arthritis and systemic lupus erythematosus. In recent years, Treg cells have become a research hotspot in the field of immunology. FOX (forkhead box) is a general term for vertebrate forkhead-like transcription factors. It is a large family of transcription factors with multiple functions, usually related to the regulation of cell growth and development. Foxp3 is a member of the forkhead-like transcription factor family. Studies have shown that Foxp3 is a key transcriptional regulator protein that determines the differentiation and function of Treg cells, and is mainly expressed in natural and natural regulatory T cells (nTreg) and inducible regulatory T cells (iTreg). In the process of inflammation, Foxp3 down-regulation can make Treg cells obtain effector T cell-like functions. But this molecular mechanism is not very clear at present. In this article, the researchers confirmed that the stress signals triggered by proinflammatory cytokines and lipopolysaccharides cause the degradation of Foxp3 through the action of the E3 ubiquitin ligase Stub1. Stub1 interacts with Foxp3 and promotes its K48 polyubiquitination in an Hsp70-dependent manner. The researchers found that inhibiting endogenous Stub1 or Hsp70 can prevent Foxp3 degradation. Moreover, overexpression of Stub1 in Treg cells can destroy the ability of Treg cells to suppress inflammatory immune responses in vivo and in vivo, conferring its Th1 cell-like phenotype. These results indicate that the pressure-activated Stub1-Hsp70 complex plays an important role in promoting Treg cell inactivation, thereby providing a potential new target for therapeutic intervention in autoimmune diseases, infections and cancer.
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December 08, 2020