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| Verfasst von: | Glöckner, Nina [VerfasserIn]  |
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| | Zur Oven-Krockhaus, Sven [VerfasserIn] |
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| | Rohr, Leander [VerfasserIn] |
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| | Wackenhut, Frank [VerfasserIn] |
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| | Burmeister, Moritz [VerfasserIn] |
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| | Wanke, Friederike [VerfasserIn] |
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| | Holzwart, Eleonore [VerfasserIn] |
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| | Meixner, Alfred J. [VerfasserIn] |
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| | Wolf, Sebastian [VerfasserIn] |
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| | Harter, Klaus [VerfasserIn] |
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| Titel: | Three-fluorophore FRET enables the analysis of ternary protein association in living plant cells |
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| Verf.angabe: | 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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| E-Jahr: | 2022 |
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| Jahr: | 6 October 2022 |
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| Umfang: | 18 S. |
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| Fussnoten: | Gesehen am 04.01.2023 |
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| Titel Quelle: | Enthalten in: Plants |
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| Ort Quelle: | Basel : MDPI, 2012 |
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| Jahr Quelle: | 2022 |
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| Band/Heft Quelle: | 11(2022), 19 vom: Okt., Artikel-ID 2630, Seite 1-18 |
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| ISSN Quelle: | 2223-7747 |
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| Abstract: | 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. |
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| DOI: | doi:10.3390/plants11192630 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext: https://doi.org/10.3390/plants11192630 |
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| | Volltext: https://www.mdpi.com/2223-7747/11/19/2630 |
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| | DOI: https://doi.org/10.3390/plants11192630 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | FRET-fluorescence lifetime imaging microscopy (FRET-FLIM) |
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| | nanodomains |
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| | plasma membrane |
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| | protein-protein interaction |
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| | spectral Förster resonance energy transfer (FRET) |
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| K10plus-PPN: | 1830367382 |
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| Verknüpfungen: | → Zeitschrift |
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Three-fluorophore FRET enables the analysis of ternary protein association in living plant cells / Glöckner, Nina [VerfasserIn]; 6 October 2022 (Online-Ressource)
