Ubiquitination is a common form of posttranslational modification that has been implicated in regulating considerable immune signaling pathways. The functions of canonic K48‐ and K63‐linked ubiquitination have been well studied.… Click to show full abstract
Ubiquitination is a common form of posttranslational modification that has been implicated in regulating considerable immune signaling pathways. The functions of canonic K48‐ and K63‐linked ubiquitination have been well studied. However, the roles of noncanonic ubiquitination remain largely unexplored and require further investigations. There is increasing evidence suggesting that K27‐linked noncanonic ubiquitination turns out to be indispensable to both innate immune signaling and T cell signaling. In this review, we provide an overview of the latest findings related to K27‐linked ubiquitination, and highlight the crucial roles of K27‐linked ubiquitination in regulating antimicrobial response, cytokine signaling and response, as well as T cell activation and differentiation. We also propose interesting areas for better understanding how K27‐linked ubiquitination regulates immunity.
               
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