Membralin is required for maize development and defines a branch of the endoplasmic reticulum-associated degradation pathway in plants.

Endoplasmic reticulum (ER)-associated degradation (ERAD) plays key roles in controlling protein levels and quality in eukaryotes. The Ring Finger Protein 185 (RNF185)/membralin ubiquitin ligase complex was recently identified as a branch in mammals and is essential for neuronal function, but its function in plant development is unknown. Here, we report the map-based cloning and characterization of (), which encodes the ER membrane-localized protein membralin and specifically interacts with maize homologs of RNF185 and related components. The mutant shows defective leaf and root development due to reduced cell number. The defects of were largely restored by expressing membralin genes from and mice, highlighting the conserved roles of membralin proteins in animals and plants. The excessive accumulation of β-hydroxy β-methylglutaryl-CoA reductase in indicates that the enzyme is a membralin-mediated ERAD target. The activation of mRNA splicing-related unfolded protein response signaling and marker gene expression in , as well as DNA fragment and cell viability assays, indicate that membralin deficiency induces ER stress and cell death in maize, thereby affecting organogenesis. Our findings uncover the conserved, indispensable role of the membralin-mediated branch of the ERAD pathway in plants. In addition, contributes to plant architecture in a dose-dependent manner, which can serve as a potential target for genetic engineering to shape ideal plant architecture, thereby enhancing high-density maize yields.