A hetero-oligomeric remorin-receptor complex regulates plant development
Abel, N. B.; Buschle, C. A.; Hernandez-Ryes, C.; Burkart, S. S.; Deroubaix, A.-F.; Mergner, J.; Gronnier, J.; Jarsch, I. K.; Folgmann, J.; Braun, K. H.; Bayer, E.; Germain, V.; Derbyshire, P.; Menke, F. L. H.; Kemmerling, B.; Zipfel, C.; Kuester, B.; Mongrand, S.; Marin, M.; Ott, T.
Show abstract
Plant growth and development are modulated by both biotic and abiotic stress. Increasing evidence suggests that cellular integration of the corresponding signals occurs within preformed hubs at the plasma membrane called nanodomains. These membrane sub-compartments are organized by multivalent molecular scaffold proteins, such as remorins. Here, we demonstrate that Group 1 remorins form a hetero-oligomeric complex at the plasma membrane. While these remorins are functionally redundant for some pathways their multivalency also allows the recruitment of specific interaction partners. One of them, the receptor-like kinase REMORIN-INTERACTING RECEPTOR 1 (RIR1), that acts redundantly with the closely related receptor NILR2, is specifically recruited by REM1.2 in a phosphorylation-dependent manner. Overlapping developmental phenotypes suggest that the REM/RIR complex regulates key developmental pathways.
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