Furthermore, our results explain how cells maintain IRF3 stability under uninfected conditions, as the constitutive binding of TRIM71 to IRF3 suggests that IRF3 may maintain itself in the resting state through weak linear ubiquitination modifications and that after viral infection, DYRK4 recruits more TRIM71 and LUBAC to enhance interactions with IRF3 for increased linear ubiquitination to maintain IRF3 stability and enhance the antiviral response. This evidence concerns the gene DYRK4 and viral infectious disease.