Evidence map›Paper›PMID 36235497›Full record

ArticlePlants (Basel, Switzerland)2022

Three-Fluorophore FRET Enables the Analysis of Ternary Protein Association in Living Plant Cells.

Nina Glöckner, Sven Zur Oven-Krockhaus, Leander Rohr, Frank Wackenhut, Moritz Burmeister, Friederike Wanke, Eleonore Holzwart, Alfred J Meixner, Sebastian Wolf, Klaus Harter

Open access · goldAbstract read
In one paragraph

Article in Plants (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.4field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 27 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Nina GlöcknerCenter for Plant Molecular Biology (ZMBP), University of Tübingen, 72076 Tübingen, Germany.
Sven Zur Oven-KrockhausCenter for Plant Molecular Biology (ZMBP), University of Tübingen, 72076 Tübingen, Germany.
Leander RohrCenter for Plant Molecular Biology (ZMBP), University of Tübingen, 72076 Tübingen, Germany.ORCID 0000-0003-4592-4197
Frank WackenhutInstitute for Physical & Theoretical Chemistry, University of Tübingen, 72076 Tübingen, Germany.ORCID 0000-0001-6554-6600
Moritz BurmeisterInstitute for Physical & Theoretical Chemistry, University of Tübingen, 72076 Tübingen, Germany.ORCID 0000-0003-3980-0753
Friederike WankeCenter for Plant Molecular Biology (ZMBP), University of Tübingen, 72076 Tübingen, Germany.
Eleonore HolzwartCentre for Organismal Studies (COS), University of Heidelberg, 69117 Heidelberg, Germany.
Alfred J MeixnerInstitute for Physical & Theoretical Chemistry, University of Tübingen, 72076 Tübingen, Germany.
Sebastian WolfCenter for Plant Molecular Biology (ZMBP), University of Tübingen, 72076 Tübingen, Germany.ORCID 0000-0003-0832-6315
Klaus HarterCenter for Plant Molecular Biology (ZMBP), University of Tübingen, 72076 Tübingen, Germany.ORCID 0000-0002-2150-6970
University of Tübingen · DEHeidelberg University · DE

Funding

Deutsche Forschungsgemeinschaft CRC 1101/D02,Z02; WO 1660/6; HA 2146/22; ME 1600/13; INST 37/819-1 FUGG; INST 37/965-1 FUGG
6 · The paper itself

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.

Indexed as

FRET-fluorescence lifetime imaging microscopy (FRET-FLIM)nanodomainsplasma membraneprotein-protein interactionspectral Förster resonance energy transfer (FRET)

Identifiers

PMID36235497
PMCPMC9571070
OpenAlexW2965752285

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.