| Autor: |
Bücherl CA; The Sainsbury Laboratory, Norwich Research Park, Norwich, United Kingdom., Jarsch IK; Ludwig-Maximilians-Universität München, Institute of Genetics, Martinsried, Germany., Schudoma C; The Sainsbury Laboratory, Norwich Research Park, Norwich, United Kingdom., Segonzac C; The Sainsbury Laboratory, Norwich Research Park, Norwich, United Kingdom., Mbengue M; The Sainsbury Laboratory, Norwich Research Park, Norwich, United Kingdom., Robatzek S; The Sainsbury Laboratory, Norwich Research Park, Norwich, United Kingdom., MacLean D; The Sainsbury Laboratory, Norwich Research Park, Norwich, United Kingdom., Ott T; Ludwig-Maximilians-Universität München, Institute of Genetics, Martinsried, Germany., Zipfel C; The Sainsbury Laboratory, Norwich Research Park, Norwich, United Kingdom. |
| Abstrakt: |
Cell surface receptors govern a multitude of signalling pathways in multicellular organisms. In plants, prominent examples are the receptor kinases FLS2 and BRI1, which activate immunity and steroid-mediated growth, respectively. Intriguingly, despite inducing distinct signalling outputs, both receptors employ common downstream signalling components, which exist in plasma membrane (PM)-localised protein complexes. An important question is thus how these receptor complexes maintain signalling specificity. Live-cell imaging revealed that FLS2 and BRI1 form PM nanoclusters. Using single-particle tracking we could discriminate both cluster populations and we observed spatiotemporal separation between immune and growth signalling platforms. This finding was confirmed by visualising FLS2 and BRI1 within distinct PM nanodomains marked by specific remorin proteins and differential co-localisation with the cytoskeleton. Our results thus suggest that signalling specificity between these pathways may be explained by the spatial separation of FLS2 and BRI1 with their associated signalling components within dedicated PM nanodomains. |
