Nature Communications , 2023, 14 (1),

Stabilization of membrane topologies by proteinaceous remorin scaffolds

Su, C. | Rodriguez-Franco, M. | Lace, B. | Nebel, N. | Hernandez-Reyes, C. | Liang, P. | Schulze, E. | Mymrikov, E. V. | Gross, N. M. | Knerr, J. | Wang, H. | Siukstaite, L. | Keller, J. | Libourel, C. | Fischer, A. A. M. | Gabor, K. E. | Mark, E. | Popp, C. | Hunte, C. | Weber, Wilfried | Wendler, P. | Stanislas, T. | Delaux, P. M. | Einsle, O. | Grosse, R. | Römer, W. | Ott, T.

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. © 2023, The Author(s).

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