1. Substrate recognition by TRIM and TRIM-like proteins in innate immunity
- Author
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Sun Hur and Hai-Tao Wang
- Subjects
0301 basic medicine ,RIG-I like receptors ,Interferon-Induced Helicase, IFIH1 ,animal structures ,Ubiquitin-Protein Ligases ,viruses ,Substrate recognition ,B30.2-SPRY Domain ,Biology ,Article ,Trim ,Substrate Specificity ,Tripartite Motif Proteins ,03 medical and health sciences ,0302 clinical medicine ,Tripartite Motif ,Humans ,Tripartite motif protein ,Receptors, Immunologic ,Adaptor Proteins, Signal Transducing ,Innate immunity ,Innate immune system ,Intracellular Signaling Peptides and Proteins ,RNA ,Cell Biology ,Immunity, Innate ,Cell biology ,030104 developmental biology ,Gene Expression Regulation ,Oligomer ,Multigene Family ,DEAD Box Protein 58 ,Interferon Regulatory Factor-3 ,Signal transduction ,PRY-SPRY domain ,030217 neurology & neurosurgery ,Signal Transduction ,Developmental Biology - Abstract
TRIM (Tripartite motif) and TRIM-like proteins have emerged as an important class of E3 ligases in innate immunity. Their functions range from activation or regulation of innate immune signaling pathway to direct detection and restriction of pathogens. Despite the importance, molecular mechanisms for many TRIM/TRIM-like proteins remain poorly characterized, in part due to challenges of identifying their substrates. In this review, we discuss several TRIM/TRIM-like proteins in RNA sensing pathways and viral restriction functions. We focus on those containing PRY-SPRY, the domain most frequently used for substrate recognition, and discuss emerging mechanisms that are commonly utilized by several TRIM/TRIM-like proteins to tightly control their interaction with the substrates.
- Published
- 2021
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