Unraveling Protein-Protein Interactions with Precision: Insights from FLIM-FRET Technique

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F25%3A00143777" target="_blank" >RIV/00216224:14740/25:00143777 - isvavai.cz</a>

Výsledek na webu

<a href="https://olomouc.ueb.cas.cz/en/cpnw-programme" target="_blank" >https://olomouc.ueb.cas.cz/en/cpnw-programme</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Unraveling Protein-Protein Interactions with Precision: Insights from FLIM-FRET Technique

Popis výsledku v původním jazyce

FLIM-FRET (Fluorescence Lifetime Imaging Microscopy–Förster Resonance Energy Transfer) analysis has revolutionized the study of plant protein complexes by allowing real-time, high-resolution visualization and quantification of protein-protein interactions in living cells. By precisely measuring fluorescence lifetime changes, this technique provides a robust platform for dissecting the molecular architecture of nuclear protein assemblies and dynamic signaling pathways. In this study, we first demonstrate how Telomere Repeat-Binding proteins in Physcomitrella patens assemble into distinct nuclear complexes via homo- and heterodimerization in nucleoplasmic foci. We then apply FLIM-FRET to investigate cytokinin signaling events by showing that phosphorylation of Arabidopsis Histidine Phosphotransfer Protein 3 at a specific serine motif critically influences its binding to other cytokinin signaling components. Collectively, these findings underscore the versatility of FLIM-FRET for studying both dynamic protein complexes and signaling pathways, offering new insights into the molecular mechanisms under various physiological and environmental conditions.

Název v anglickém jazyce

Unraveling Protein-Protein Interactions with Precision: Insights from FLIM-FRET Technique

Popis výsledku anglicky

FLIM-FRET (Fluorescence Lifetime Imaging Microscopy–Förster Resonance Energy Transfer) analysis has revolutionized the study of plant protein complexes by allowing real-time, high-resolution visualization and quantification of protein-protein interactions in living cells. By precisely measuring fluorescence lifetime changes, this technique provides a robust platform for dissecting the molecular architecture of nuclear protein assemblies and dynamic signaling pathways. In this study, we first demonstrate how Telomere Repeat-Binding proteins in Physcomitrella patens assemble into distinct nuclear complexes via homo- and heterodimerization in nucleoplasmic foci. We then apply FLIM-FRET to investigate cytokinin signaling events by showing that phosphorylation of Arabidopsis Histidine Phosphotransfer Protein 3 at a specific serine motif critically influences its binding to other cytokinin signaling components. Collectively, these findings underscore the versatility of FLIM-FRET for studying both dynamic protein complexes and signaling pathways, offering new insights into the molecular mechanisms under various physiological and environmental conditions.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10611 - Plant sciences, botany

Projekt

<a href="/cs/project/LUAUS24277" target="_blank" >LUAUS24277: Objasnění mechanismů hormonálních regulací longitudinální zonace kořene</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2025

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů