Evidence map›Paper›PMID 26157163›Full record

ArticleMolecular biology of the cell2015

Regulation of TGF-β receptor hetero-oligomerization and signaling by endoglin.

Leslie Pomeraniec, Melissa Hector-Greene, Marcelo Ehrlich, Gerard C Blobe, Yoav I Henis

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
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  5. Article
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  8. Review
  9. Article
  10. TGF-β superfamily co-receptors in cancer.Developmental dynamics : an official publication of the American Association of Anatomists · 2022
    Review
  11. Article
  12. [Hereditary hemorrhagic telangiectasia: 8 case report and lirerature review].Lin chuang er bi yan hou tou jing wai ke za zhi = Journal of clinical otorhinolaryngology head and neck surgery · 2021
    Article
  13. Article
  14. Article
  15. The Role of Endoglin in Hepatocellular Carcinoma.International journal of molecular sciences · 2021
    Review
  16. Endoglin in the Spotlight to Treat Cancer.International journal of molecular sciences · 2021
    Review
  17. Article
  18. Review
  19. Review
  20. 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

5 authors at 2 institutions in 2 countries.

Leslie PomeraniecDepartment of Neurobiology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.
Melissa Hector-GreeneDepartment of Medicine, Duke University Medical Center, Durham, NC 27708.
Marcelo EhrlichDepartment of Cell Research and Immunology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.
Gerard C BlobeDepartment of Medicine, Duke University Medical Center, Durham, NC 27708.
Yoav I HenisDepartment of Neurobiology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel henis@post.tau.ac.il.
Tel Aviv University · ILDuke Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Complex formation among transforming growth factor-β (TGF-β) receptors and its modulation by coreceptors represent an important level of regulation for TGF-β signaling. Oligomerization of ALK5 and the type II TGF-β receptor (TβRII) has been thoroughly investigated, both in vitro and in intact cells. However, such studies, especially in live cells, are missing for the endothelial cell coreceptor endoglin and for the ALK1 type I receptor, which enables endothelial cells to respond to TGF-β by activation of both Smad2/3 and Smad1/5/8. Here we combined immunoglobulin G-mediated immobilization of one cell-surface receptor with lateral mobility studies of a coexpressed receptor by fluorescence recovery after photobleaching (FRAP) to demonstrate that endoglin forms stable homodimers that function as a scaffold for binding TβRII, ALK5, and ALK1. ALK1 and ALK5 bind to endoglin with differential dependence on TβRII, which plays a major role in recruiting ALK5 to the complex. Signaling data indicate a role for the quaternary receptor complex in regulating the balance between TGF-β signaling to Smad1/5/8 and to Smad2/3.

Indexed as

Activin Receptors, Type IIAnimalsAntigens, CDChlorocebus aethiopsCOS CellsEndoglinEndothelial CellsFluorescence Recovery After PhotobleachingHumansProtein BindingProtein Serine-Threonine KinasesReceptors, Cell SurfaceReceptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type ISignal TransductionSmad ProteinsActivin Receptors, Type IIACVRL1 protein, humanAntigens, CDEndoglinENG protein, humanProtein Serine-Threonine KinasesReceptors, Cell SurfaceReceptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type ISmad ProteinsTGFBR1 protein, humanTransforming Growth Factor beta

Identifiers

PMID26157163
PMCPMC4551323
OpenAlexW2130000320

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.