Evidence map›Paper›PMID 29376829›Full record

ArticleeLife2018

TGF-β uses a novel mode of receptor activation to phosphorylate SMAD1/5 and induce epithelial-to-mesenchymal transition.

Anassuya Ramachandran, Pedro Vizán, Debipriya Das, Probir Chakravarty, Janis Vogt, Katherine W Rogers, Patrick Müller, Andrew P Hinck, Gopal P Sapkota, Caroline S Hill

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
9.7field-weighted citation impact, top 1% 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

119 citing papers in PubMed, 201 citations in OpenAlex.

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59 more citing papers are in PubMed but not listed here.

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 4 institutions in 3 countries.

Anassuya RamachandranDevelopmental Signalling Laboratory, The Francis Crick Institute, London, United Kingdom.ORCID http://orcid.org/0000-0002-0123-6539
Pedro VizánDevelopmental Signalling Laboratory, The Francis Crick Institute, London, United Kingdom.
Debipriya DasDevelopmental Signalling Laboratory, The Francis Crick Institute, London, United Kingdom.
Probir ChakravartyBioinformatics and Biostatistics Facility, The Francis Crick Institute, London, United Kingdom.
Janis VogtMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, United Kingdom.
Katherine W RogersFriedrich Miescher Laboratory of the Max Planck Society, Tübingen, Germany.ORCID http://orcid.org/0000-0001-5700-2662
Patrick MüllerFriedrich Miescher Laboratory of the Max Planck Society, Tübingen, Germany.ORCID http://orcid.org/0000-0002-0702-6209
Andrew P HinckDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, United States.
Gopal P SapkotaMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, United Kingdom.ORCID http://orcid.org/0000-0001-9931-3338
Caroline S HillDevelopmental Signalling Laboratory, The Francis Crick Institute, London, United Kingdom.ORCID http://orcid.org/0000-0002-8632-0480
The Francis Crick Institute · GBMax Planck Society · DEUniversity of Dundee · GBUniversity of Pittsburgh · US

Funding

LIGAND/RECEPTOR INTERACTIONS IN THE TGF BETA SUPERFAMILYR01GM058670 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI HINCK, ANDREW P · 1999 to 2017
$3.6M
Inhibition of the tumor-promoting effects of TGF-beta in advanced prostate cancerR01CA172886 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI HINCK, ANDREW P, SUN, LUZHE · 2013 to 2016
$1.2M
Cancer Research UK 15681Cancer Research UK FC001095Medical Research Council FC001095Medical Research Council MC_UU_00018/6Medical Research Council MC_UU_12016/3NCI NIH HHS CA172886NCI NIH HHS R01 CA172886NIGMS NIH HHS GM58670NIGMS NIH HHS R01 GM058670Wellcome TrustWellcome Trust FC001095
6 · The paper itself

Abstract

The best characterized signaling pathway downstream of transforming growth factor β (TGF-β) is through SMAD2 and SMAD3. However, TGF-β also induces phosphorylation of SMAD1 and SMAD5, but the mechanism of this phosphorylation and its functional relevance is not known. Here, we show that TGF-β-induced SMAD1/5 phosphorylation requires members of two classes of type I receptor, TGFBR1 and ACVR1, and establish a new paradigm for receptor activation where TGFBR1 phosphorylates and activates ACVR1, which phosphorylates SMAD1/5. We demonstrate the biological significance of this pathway by showing that approximately a quarter of the TGF-β-induced transcriptome depends on SMAD1/5 signaling, with major early transcriptional targets being the

Indexed as

Epithelial-Mesenchymal TransitionProtein Processing, Post-TranslationalActivin Receptors, Type IAnimalsCell LineGene Expression ProfilingGene Regulatory NetworksHumansInhibitor of Differentiation Protein 1PhosphorylationReceptor, Transforming Growth Factor-beta Type ISmad1 ProteinSmad5 ProteinTransforming Growth Factor betaActivin Receptors, Type IACVR1 protein, humanID1 protein, humanInhibitor of Differentiation Protein 1Receptor, Transforming Growth Factor-beta Type ISmad1 ProteinSmad5 ProteinTransforming Growth Factor betaACVR1biochemistrycell biologychemical biologyepithelial-to-mesenchymal transitionhumanID genesmouseSMAD1/5TGF-beta

Identifiers

PMID29376829
PMCPMC5832415
OpenAlexW2787586915

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.