Figure 5.

Role of LLPS in immune signaling. (A). Double-stranded DNA binding with cGAS prominently promoted their phase separation and the formation of condensates. In these condensates, cGAS is highly concentrated, which further promotes its catalytic activity by changing the multivalence interaction between cGAS and DNA. (B). The TCR complex is phosphorylated by LCK on ITAM domain, which further recruits the kinase ZAP70. The transmembrane protein LAT is then phosphorylated by ZAP70 and drives LLPS through multivalent interactions with GRB2 and SOS1 for MAPK signaling. (C). SLP65 and its binding partner CIN85 form LLPS condensates in the cytosol of B cells through multivalent interactions between the SLP65 and CIN85.