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We recently revealed that diacylglycerol (DG) kinase (DGK) \u03b4 induces ubiquitination\/degradation of SERT in a DGK activity\u2010dependent manner through Praja\u20101 E3 ubiquitin\u2010protein ligase. However, it is still unclear how Praja\u20101 activity is regulated by DGK\u03b4. Here, we reveal that 1\u2010stearoyl\u20102\u2010docosahexaenoyl (18:0\/22:6)\u2010phosphatidic acid (PA) and 18:0\/22:6\u2010DG are simultaneously decreased and accumulated, respectively, in the DGK\u03b4\u2010knockout mouse brain, indicating that DGK\u03b4 selectively phosphorylates 18:0\/22:6\u2010DG to generate 18:0\/22:6\u2010PA. Moreover, we find that 18:0\/22:6\u2010PA selectively binds to Praja\u20101 and enhances its activity. 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