Evidence map›Paper›PMID 12021305›Full record

ArticleThe Journal of experimental medicine2002

Disruption of transforming growth factor beta signaling by a novel ligand-dependent mechanism.

Tania Fernandez, Stephanie Amoroso, Shellyann Sharpe, Gary M Jones, Valery Bliskovski, Alexander Kovalchuk, Lalage M Wakefield, Seong-Jin Kim, Michael Potter, John J Letterio

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

10 citing papers in PubMed, 40 citations in OpenAlex.

  1. Extracellular matrix and its therapeutic potential for cancer treatment.Signal transduction and targeted therapy · 2021
    Review
  2. Article
  3. Article
  4. Review
  5. Targeting TGF-β signaling in cancer.Expert opinion on therapeutic targets · 2013
    Review
  6. TGF-β - an excellent servant but a bad master.Journal of translational medicine · 2012
    Review
  7. Article
  8. Article
  9. Article
  10. Review
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 1 institution in 1 country.

Tania FernandezLaboratory of Cell Regulation and Carcinogenesis, The National Cancer Institute, The National Institutes of Health, Bethesda, MD 20892, USA.
Stephanie Amoroso
Shellyann Sharpe
Gary M Jones
Valery Bliskovski
Alexander Kovalchuk
Lalage M Wakefield
Seong-Jin Kim
Michael Potter
John J Letterio
National Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transforming growth factor (TGF)-beta is the prototype in a family of secreted proteins that act in autocrine and paracrine pathways to regulate cell development and function. Normal cells typically coexpress TGF-beta receptors and one or more isoforms of TGF-beta, thus the synthesis and secretion of TGF-beta as an inactive latent complex is considered an essential step in regula-ting the activity of this pathway. To determine whether intracellular activation of TGF-beta results in TGF-beta ligand-receptor interactions within the cell, we studied pristane-induced plasma cell tumors (PCTs). We now demonstrate that active TGF-beta1 in the PCT binds to intracellular TGF-beta type II receptor (TbetaRII). Disruption of the expression of TGF-beta1 by antisense TGF-beta1 mRNA restores localization of TbetaRII at the PCT cell surface, indicating a ligand-induced impediment in receptor trafficking. We also show that retroviral expression of a truncated, dominant-negative TbetaRII (dnTbetaRII) effectively competes for intracellular binding of active ligand in the PCT and restores cell surface expression of the endogenous TbetaRII. Analysis of TGF-beta receptor-activated Smad2 suggests the intracellular ligand-receptor complex is not capable of signaling. These data are the first to demonstrate the formation of an intracellular TGF-beta-receptor complex, and define a novel mechanism for modulating the TGF-beta signaling pathway.

Indexed as

AnimalsAutocrine CommunicationBlotting, WesternCell MembraneDNA-Binding ProteinsLigandsMicePlasmacytomaProtein BindingProtein Serine-Threonine KinasesProtein TransportReceptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type IIRNA, AntisenseSignal TransductionSmad2 ProteinDNA-Binding ProteinsLigandspristaneProtein Serine-Threonine KinasesReceptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type IIRNA, AntisenseSmad2 ProteinSmad2 protein, mouseTerpenesTrans-ActivatorsTransforming Growth Factor beta

Identifiers

PMID12021305
PMCPMC2193757
OpenAlexW2086326400

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.