The biogenesis of membrane and secretory proteins is precisely governed by endoplasmic reticulum-associated ribosome quality control (ER-RQC). UFMylation of ribosomal protein RPL26 is known to play a critical role in the ER-RQC pathway. However, the regulatory mechanisms orchestrating UFMylation and the ER-RQC pathway remain largely elusive. Therefore, this study aims to deeply elucidate whether and how PRMT1 influence the ER-RQC.