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

a 2025

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

SKALÁK, Jan; Alžbeta KUSOVÁ; Petra SCHRUMPFOVÁ a Jan HEJÁTKO

Základní údaje

Originální název

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

Autoři

SKALÁK, Jan; Alžbeta KUSOVÁ; Petra SCHRUMPFOVÁ a Jan HEJÁTKO

Vydání

The Czech Plant Nucleus Workshop, 2025

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10611 Plant sciences, botany

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14740/25:00143777

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

FLIM-FRET; protein; interactions; plant; cytokinins; signaling

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 26. 2. 2026 09:26, Mgr. Eva Dubská

Anotace

V originále

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.

Návaznosti

LUAUS24277, projekt VaV

Název: Objasnění mechanismů hormonálních regulací longitudinální zonace kořene

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Objasnění mechanismů hormonálních regulací longitudinální zonace kořene, INTER-ACTION (USA)

Přiložené soubory

The_Czech_Plant_Nucleus_Workshop__26.-27.5._2025.pdf

Citovat

SKALÁK, Jan; Alžbeta KUSOVÁ; Petra SCHRUMPFOVÁ a Jan HEJÁTKO. Unraveling Protein-Protein Interactions with Precision: Insights from FLIM-FRET Technique. In The Czech Plant Nucleus Workshop. 2025.

@proceedings{2556817,
   author = {Skalák, Jan and Kusová, Alžbeta and Schrumpfová, Petra and Hejátko, Jan},
   booktitle = {The Czech Plant Nucleus Workshop},
   keywords = {FLIM-FRET; protein; interactions; plant; cytokinins; signaling},
   language = {eng},
   title = {Unraveling Protein-Protein Interactions with Precision: Insights from FLIM-FRET Technique},
   url = {https://olomouc.ueb.cas.cz/en/cpnw-programme},
   year = {2025}
}

TY  - CONF
ID  - 2556817
AU  - Skalák, Jan - Kusová, Alžbeta - Schrumpfová, Petra - Hejátko, Jan
PY  - 2025
TI  - Unraveling Protein-Protein Interactions with Precision: Insights from FLIM-FRET Technique
KW  - FLIM-FRET
KW  - protein
KW  - interactions
KW  - plant
KW  - cytokinins
KW  - signaling
UR  - https://olomouc.ueb.cas.cz/en/cpnw-programme
N2  - 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.
ER  -

SKALÁK, Jan; Alžbeta KUSOVÁ; Petra SCHRUMPFOVÁ a Jan HEJÁTKO. Unraveling Protein-Protein Interactions with Precision: Insights from FLIM-FRET Technique. In \textit{The Czech Plant Nucleus Workshop}. 2025.

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