Three-fluorophore FRET enables the analysis of ternary protein association in living plant cells
Protein-protein interaction studies provide valuable insights into cellular signaling. Brassinosteroid (BR) signaling is initiated by the hormone-binding receptor Brassinosteroid Insensitive 1 (BRI1) and its co-receptor BRI1 Associated Kinase 1 (BAK1). BRI1 and BAK1 were shown to interact independen...
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| Hauptverfasser: | , , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
6 October 2022
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| In: |
Plants
Year: 2022, Jahrgang: 11, Heft: 19, Pages: 1-18 |
| ISSN: | 2223-7747 |
| DOI: | 10.3390/plants11192630 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.3390/plants11192630 Verlag, lizenzpflichtig, Volltext: https://www.mdpi.com/2223-7747/11/19/2630 
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| Verfasserangaben: | Nina Glöckner, Sven zur Oven-Krockhaus, Leander Rohr, Frank Wackenhut, Moritz Burmeister, Friederike Wanke, Eleonore Holzwart, Alfred J. Meixner, Sebastian Wolf an Klaus Harter |
MARC
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| 245 | 1 | 0 | |a Three-fluorophore FRET enables the analysis of ternary protein association in living plant cells |c Nina Glöckner, Sven zur Oven-Krockhaus, Leander Rohr, Frank Wackenhut, Moritz Burmeister, Friederike Wanke, Eleonore Holzwart, Alfred J. Meixner, Sebastian Wolf an Klaus Harter |
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| 520 | |a Protein-protein interaction studies provide valuable insights into cellular signaling. Brassinosteroid (BR) signaling is initiated by the hormone-binding receptor Brassinosteroid Insensitive 1 (BRI1) and its co-receptor BRI1 Associated Kinase 1 (BAK1). BRI1 and BAK1 were shown to interact independently with the Receptor-Like Protein 44 (RLP44), which is implicated in BRI1/BAK1-dependent cell wall integrity perception. To demonstrate the proposed complex formation of BRI1, BAK1 and RLP44, we established three-fluorophore intensity-based spectral Förster resonance energy transfer (FRET) and FRET-fluorescence lifetime imaging microscopy (FLIM) for living plant cells. Our evidence indicates that RLP44, BRI1 and BAK1 form a ternary complex in a distinct plasma membrane nanodomain. In contrast, although the immune receptor Flagellin Sensing 2 (FLS2) also forms a heteromer with BAK1, the FLS2/BAK1 complexes are localized to other nanodomains. In conclusion, both three-fluorophore FRET approaches provide a feasible basis for studying the in vivo interaction and sub-compartmentalization of proteins in great detail. | ||
| 650 | 4 | |a FRET-fluorescence lifetime imaging microscopy (FRET-FLIM) | |
| 650 | 4 | |a nanodomains | |
| 650 | 4 | |a plasma membrane | |
| 650 | 4 | |a protein-protein interaction | |
| 650 | 4 | |a spectral Förster resonance energy transfer (FRET) | |
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| 700 | 1 | |a Rohr, Leander |e VerfasserIn |4 aut | |
| 700 | 1 | |a Wackenhut, Frank |e VerfasserIn |4 aut | |
| 700 | 1 | |a Burmeister, Moritz |e VerfasserIn |4 aut | |
| 700 | 1 | |a Wanke, Friederike |e VerfasserIn |4 aut | |
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| 700 | 1 | |a Harter, Klaus |e VerfasserIn |4 aut | |
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