AP-1和PRMT1是细胞进程中至关重要的分子，但是这些蛋白质在细胞功能上的相互作用还不太清楚。胃癌是全球一种恶性疾病。对胃肿瘤发生机制的深入了解仍然是模糊的。在这项研究中，我们发现PRMT1直接与c-Fos相互作用，增强AP-1的激活。PRMT1介导的c-Fos的精氨酸甲基化（单甲基化和双甲基化）协同增强了c-Fos介导的AP-1活性，因此增加了c-Fos蛋白的稳定性。与此发现一致，PRMT1敲降降低了c-Fos蛋白水平。我们发现c-Fos蛋白经历自噬降解，并发现PRMT1介导的R287甲基化保护c-Fos免受自噬体降解的影响，并与胃肿瘤的临床病理学变量和预后相关。综上所述，我们的数据表明PRMT1介导的c-Fos蛋白稳定促进了胃肿瘤的发生。我们认为针对这种修饰可能构成胃癌的新治疗策略。© 作者（们）。

Both AP-1 and PRMT1 are vital molecules in variety of cellular progresssion, but the interaction between these proteins in the context of cellular functions is less clear. Gastric cancer (GC) is one of the pernicious diseases worldwide. An in-depth understanding of the molecular mode of action underlying gastric tumorigenesis is still elusive. In this study, we found that PRMT1 directly interacts with c-Fos and enhances AP-1 activation. PRMT1-mediated arginine methylation (mono- and dimethylation) of c-Fos synergistically enhances c-Fos-mediated AP-1 liveliness and consequently increases c-Fos protein stabilization. Consistent with this finding, PRMT1 knockdown decreases the protein level of c-Fos. We discovered that the c-Fos protein undergoes autophagic degradation and found that PRMT1-mediated methylation at R287 protects c-Fos from autophagosomal degradation and is linked to clinicopathologic variables as well as prognosis in stomach tumor. Together, our data demonstrate that PRMT1-mediated c-Fos protein stabilization promotes gastric tumorigenesis. We contend that targeting this modification could constitute a new therapeutic strategy in gastric cancer.© The author(s).