Abstract
The tripartite motif (TRIM) proteins have been intensively studied as essential modulators in various biological processes, especially in regulating a wide range of signaling pathways involved in immune responses. Most TRIM proteins have E3 ubiquitin ligase activity, mediating polyubiquitination of target proteins. Emerging evidence demonstrates that TRIM proteins play important roles in innate immunity by regulating pattern recognition receptors, vital adaptor proteins, kinases, and transcription factors in innate immune signaling pathways. Additionally, the critical roles of TRIM proteins in adaptive immunity, especially in T cell development and activation, are increasingly appreciated. In this review, we aim to summarize the studies on TRIMs in both innate and adaptive immunity, focusing on their E3 ubiquitin ligase functions in pattern recognition receptor signaling pathways and T cell functions, shedding light on the developing new strategies for modulating innate and adaptive immune responses against invading pathogens and avoiding autoimmunity.
Highlights
The immune system, consisting of innate and adaptive immune arms, provides crucial protection for the host against infectious agents and serves as a housekeeper for immune homeostasis
The exciting acquisitions of studies exploring the regulatory roles of tripartite motif (TRIM) proteins in the innate immune response are the involvement of TRIMs in the cross-regulation of innate immune signal pathways, which finely orchestrates host’s innate immune responses against invading microorganisms
TRIM38 negatively regulates TLR3/TLR4-mediated IFN-I production by targeting NAP1 and TIR domain-containing adaptor protein inducing IFNb (TRIF) for ubiquitinproteasome-mediated degradation [27, 66]; this protein involves the regulation of TNFa and IL-1b-triggered signal pathways
Summary
The immune system, consisting of innate and adaptive immune arms, provides crucial protection for the host against infectious agents and serves as a housekeeper for immune homeostasis. The ubiquitinated TRIM26 interacts with NEMO and bridges the interaction between NEMO and TBK1, which promotes the recruitment of TBK1 to MAVS, leading to activation of TBK1 and the downstream signaling pathway [67] These apparent discrepancies of TRIM26 in the regulation of virus-induced RLR signaling activation might be due to the different cell types used in those studies. It is interesting to note that several TRIM proteins play essential roles in both innate and adaptive immunity Among these TRIMs, TRIM30a, negatively regulating TLR-mediated NF-kB activation by targeting the TAK1/TAB2/TAB3 complex [37], was recently found to be involved in the regulation of T cell functions. Considering that mouse Foxp does not interact with TRIM28 [96, 97], TRIM28 regulates mouse and human Treg in different ways
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