Arginine methylation is a common posttranslational modification that modulates protein function. SCY1-like pseudokinase 1 (SCYL1) is crucial for neuronal functions and interacts with γ₂-COP to form coat protein complex I (COPI) vesicles that regulate Golgi morphology. However, the molecular mechanism by which SCYL1 is regulated remains unclear. Here, we report that the γ₂-COP-binding site of SCYL1 is arginine-methylated by protein arginine methyltransferase 1 (PRMT1) and that SCYL1 arginine methylation is important for the interaction of SCYL1 with γ₂-COP. PRMT1 was colocalized with SCYL1 in the Golgi fraction. Inhibition of PRMT1 suppressed axon outgrowth and dendrite complexity via abnormal Golgi morphology. Knockdown of SCYL1 by small interfering RNA (siRNA) inhibited axon outgrowth, and the inhibitory effect was rescued by siRNA-resistant SCYL1, but not SCYL1 mutant, in which the arginine methylation site was replaced. Thus, PRMT1 regulates Golgi morphogenesis via SCYL1 arginine methylation. We propose that SCYL1 arginine methylation by PRMT1 contributes to axon and dendrite morphogenesis in neurons.

精氨酸甲基化是调节蛋白功能的常见翻译后修饰。SCY1状假性1（SCYL1）是具有γ神经元的功能和相互作用至关重要₂ -COP以形成调节高尔基体形态外壳蛋白复合物I（COPI）的囊泡。但是，SCYL1调控的分子机制仍不清楚。在这里，我们报告中指出，γ ₂ SCYL1的的COP结合位点是精氨酸甲基化由蛋白质精氨酸甲基转移酶1（PRMT1）和SCYL1精氨酸甲基化是SCYL1与γ相互作用重要的₂-警察。PRMT1与SCYL1在高尔基体中共定位。PRMT1的抑制通过异常的高尔基体形态抑制了轴突的生长和树突的复杂性。通过小干扰RNA（siRNA）敲低SCYL1抑制轴突生长，并且通过耐siRNA的SCYL1而不是SCYL1突变体（其中精氨酸甲基化位点被取代）来挽救抑制作用。因此，PRMT1通过SCYL1精氨酸甲基化调节高尔基体形态发生。我们建议通过PRMT1 SCYL1精氨酸甲基化有助于神经元的轴突和树突形态发生。