Department of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Department of Physiology, Graduate School of Medicine, Juntendo University, Tokyo, Japan.
EMBO Rep. 2022 Feb 3;23(2):e53894. doi: 10.15252/embr.202153894. Epub 2022 Jan 19.
The endoplasmic reticulum (ER) is a central hub for the biogenesis of various organelles and lipid-containing structures. Recent studies suggest that vacuole membrane protein 1 (VMP1) and transmembrane protein 41B (TMEM41B), multispanning ER membrane proteins, regulate the formation of many of these ER-derived structures, including autophagosomes, lipid droplets, lipoproteins, and double-membrane structures for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) replication. VMP1 and TMEM41B possess a DedA domain that is widely distributed not only in eukaryotes but also in prokaryotes and predicted to adopt a characteristic structure containing two reentrant loops. Furthermore, recent studies show that both proteins have lipid scrambling activity. Based on these findings, the potential roles of VMP1 and TMEM41B in the dynamic remodeling of ER membranes and the biogenesis of ER-derived structures are discussed.
内质网(ER)是各种细胞器和含脂结构生物发生的中心枢纽。最近的研究表明,液泡膜蛋白 1(VMP1)和跨膜蛋白 41B(TMEM41B),多跨 ER 膜蛋白,调节许多这些 ER 衍生结构的形成,包括自噬体、脂滴、脂蛋白和严重急性呼吸综合征冠状病毒 2(SARS-CoV-2)复制的双膜结构。VMP1 和 TMEM41B 具有 DedA 结构域,该结构域不仅广泛存在于真核生物中,也广泛存在于原核生物中,并预测采用一种包含两个折返环的特征结构。此外,最近的研究表明这两种蛋白质都具有脂质翻转活性。基于这些发现,讨论了 VMP1 和 TMEM41B 在 ER 膜的动态重塑和 ER 衍生结构生物发生中的潜在作用。