Evidence map›Paper›PMID 26482290›Full record

ArticleAdvances in biological regulation2016

Time-resolved FRET reports FGFR1 dimerization and formation of a complex with its effector PLCγ1.

Louis Perdios, Tom D Bunney, Sean C Warren, Christopher Dunsby, Paul M W French, Edward W Tate, Matilda Katan

Open access · hybridAbstract readEvaluation Study

In one paragraph

Article in Advances in biological regulation, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

1.1field-weighted citation impact, top 23% 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

1 citing paper in PubMed, 9 citations in OpenAlex.

Drug-resistance in doxorubicin-resistant FL5.12 hematopoietic cells: elevated MDR1, drug efflux and side-population positive and decreased BCL2-family member expression.Oncotarget · 2017
Article

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

7 authors at 2 institutions in 1 country.

Louis PerdiosInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, Gower St, London WC1E 6BT, UK; Department of Chemistry, Imperial College London, South Kensington Campus, Exhibition Road, London SW7 2AZ, UK.

Tom D BunneyInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, Gower St, London WC1E 6BT, UK.

Sean C WarrenDepartment of Physics, Imperial College London, South Kensington Campus, Exhibition Road, London SW7 2AZ, UK.

Christopher DunsbyDepartment of Physics, Imperial College London, South Kensington Campus, Exhibition Road, London SW7 2AZ, UK.

Paul M W FrenchDepartment of Physics, Imperial College London, South Kensington Campus, Exhibition Road, London SW7 2AZ, UK.

Edward W TateDepartment of Chemistry, Imperial College London, South Kensington Campus, Exhibition Road, London SW7 2AZ, UK.

Matilda KatanInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, Gower St, London WC1E 6BT, UK. Electronic address: m.katan@ucl.ac.uk.

Imperial College London · GBInstitute of Structural and Molecular Biology · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E000495/1Cancer Research UK 16567Cancer Research UK A16567

6 · The paper itself

Abstract

In vitro and in vivo imaging of protein tyrosine kinase activity requires minimally invasive, molecularly precise optical probes to provide spatiotemporal mechanistic information of dimerization and complex formation with downstream effectors. We present here a construct with genetically encoded, site-specifically incorporated, bioorthogonal reporter that can be selectively labelled with exogenous fluorogenic probes to monitor the structure and function of fibroblast growth factor receptor (FGFR). GyrB.FGFR1KD.TC contains a coumermycin-induced artificial dimerizer (GyrB), FGFR1 kinase domain (KD) and a tetracysteine (TC) motif that enables fluorescent labelling with biarsenical dyes FlAsH-EDT2 and ReAsH-EDT2. We generated bimolecular system for time-resolved FRET (TR-FRET) studies, which pairs FlAsH-tagged GyrB.FGFR1KD.TC and N-terminal Src homology 2 (nSH2) domain of phospholipase Cγ (PLCγ), a downstream effector of FGFR1, fused to mTurquoise fluorescent protein (mTFP). We demonstrated phosphorylation-dependent TR-FRET readout of complex formation between mTFP.nSH2 and GyrB.FGFR1KD.TC. By further application of TR-FRET, we also demonstrated formation of the GyrB.FGFR1KD.TC homodimer by coumermycin-induced dimerization. Herein, we present a spectroscopic FRET approach to facilitate and propagate studies that would provide structural and functional insights for FGFR and other tyrosine kinases.

Indexed as

DimerizationFluorescence Resonance Energy TransferHumansPhospholipase C gammaProtein BindingReceptor, Fibroblast Growth Factor, Type 1FGFR1 protein, humanPhospholipase C gammaPLCG1 protein, humanReceptor, Fibroblast Growth Factor, Type 1Fibroblast growth factor receptorPhospholipase CγTime-resolved FRET

Identifiers

PMID26482290

DOI10.1016/j.jbior.2015.09.002

PMCPMC4739061

OpenAlexW2179302712

What OpenQuestion holds

Textmetadata

LicenceCC BY

Read underepoch 390

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.