Evidence map›Paper›PMID 21423151›Full record

ArticleThe EMBO journal2011

TGF-β signalling is mediated by two autonomously functioning TβRI:TβRII pairs.

Tao Huang, Laurent David, Valentín Mendoza, Yong Yang, Maria Villarreal, Keya De, LuZhe Sun, Xiaohong Fang, Fernando López-Casillas, Jeffrey L Wrana and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

81 citing papers in PubMed, 119 citations in OpenAlex.

  1. Article
  2. Review
  3. Molecular Engineering of the Helminth TGF-β Mimetics, TGM1 and TGM4, Reveals a Novel Antagonist of TGF-β Signaling in Fibroblasts.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Repair of Isoaspartyl Residues by PCMT1 and Kidney Fibrosis.Journal of the American Society of Nephrology : JASN · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Review

21 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

11 authors at 5 institutions in 4 countries.

Tao HuangDepartment of Biochemistry, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229-3900, USA.
Laurent David
Valentín Mendoza
Yong Yang
Maria Villarreal
Keya De
LuZhe Sun
Xiaohong Fang
Fernando López-Casillas
Jeffrey L Wrana
Andrew P Hinck
The University of Texas Health Science Center at San Antonio · USBeijing National Laboratory for Molecular Sciences · CNLunenfeld-Tanenbaum Research Institute · CAUniversidad Autónoma de la Ciudad de México · MXUniversidad Nacional Autónoma de México · MX

Funding

TISSUE CULTURE---COREP30CA054174 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Lei Zheng · 1991 to 2026
$59.1M
LIGAND/RECEPTOR INTERACTIONS IN THE TGF BETA SUPERFAMILYR01GM058670 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI HINCK, ANDREW P · 1999 to 2017
$3.6M
Targeting transforming growth factor beta for cancer treatmentR01CA075253 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI SUN, LUZHE · 1997 to 2011
$2.4M
600 MHZ NUCLEAR MAGNETIC RESONANCE SPECTROMETERS10RR013879 · NCRR · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI HINCK, ANDREW P · 2000 to 2000
$400k
NCI NIH HHS CA54174NCI NIH HHS CA75253NCI NIH HHS P30 CA054174NCI NIH HHS R01 CA075253NCRR NIH HHS RR13879NIGMS NIH HHS GM58670NIGMS NIH HHS R01 GM058670
6 · The paper itself

Abstract

Transforming growth factor (TGF)-βs are dimeric polypeptides that have vital roles in regulating cell growth and differentiation. They signal by assembling a receptor heterotetramer composed of two TβRI:TβRII heterodimers. To investigate whether the two heterodimers bind and signal autonomously, one of the TGF-β protomers was substituted to block receptor binding. The substituted dimer, TGF-β3 WD, bound the TβRII extracellular domain and recruited the TβRI with affinities indistinguishable from TGF-β3, but with one-half the stoichiometry. TGF-β3 WD was further shown to retain one-quarter to one-half the signalling activity of TGF-β3 in three established assays for TGF-β function. Single-molecule fluorescence imaging with GFP-tagged receptors demonstrated a measurable increase in the proportion of TβRI and TβRII dimers upon treatment with TGF-β3, but not with TGF-β3 WD. These results provide evidence that the two TβRI:TβRII heterodimers bind and signal in an autonomous manner. They further underscore how the TGF-βs diverged from the bone morphogenetic proteins, the ancestral ligands of the TGF-β superfamily that signal through a RI:RII:RII heterotrimer.

Indexed as

Signal TransductionAnimalsCell LineCell ProliferationHumansProtein BindingProtein Serine-Threonine KinasesReceptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type IReceptor, Transforming Growth Factor-beta Type IITransforming Growth Factor beta3Protein Serine-Threonine KinasesReceptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type IReceptor, Transforming Growth Factor-beta Type IITGFB3 protein, humanTransforming Growth Factor beta3

Identifiers

PMID21423151
PMCPMC3094126
OpenAlexW1545275730

What OpenQuestion holds

Textmetadata
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.