Stabilization of membrane topologies by proteinaceous remorin scaffolds

蛋白质 remorin 支架对膜拓扑结构的稳定

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作者:Chao Su, Marta Rodriguez-Franco, Beatrice Lace, Nils Nebel, Casandra Hernandez-Reyes, Pengbo Liang, Eija Schulze, Evgeny V Mymrikov, Nikolas M Gross, Julian Knerr, Hong Wang, Lina Siukstaite, Jean Keller, Cyril Libourel, Alexandra A M Fischer, Katharina E Gabor, Eric Mark, Claudia Popp, Carola Hunte

Abstract

In plants, the topological organization of membranes has mainly been attributed to the cell wall and the cytoskeleton. Additionally, few proteins, such as plant-specific remorins have been shown to function as protein and lipid organizers. Root nodule symbiosis requires continuous membrane re-arrangements, with bacteria being finally released from infection threads into membrane-confined symbiosomes. We found that mutations in the symbiosis-specific SYMREM1 gene result in highly disorganized perimicrobial membranes. AlphaFold modelling and biochemical analyses reveal that SYMREM1 oligomerizes into antiparallel dimers and may form a higher-order membrane scaffolding structure. This was experimentally confirmed when expressing this and other remorins in wall-less protoplasts is sufficient where they significantly alter and stabilize de novo membrane topologies ranging from membrane blebs to long membrane tubes with a central actin filament. Reciprocally, mechanically induced membrane indentations were equally stabilized by SYMREM1. Taken together we describe a plant-specific mechanism that allows the stabilization of large-scale membrane conformations independent of the cell wall.

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