Evidence map›Paper›PMID 12429842›Full record

ArticleMolecular biology of the cell2002

Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit.

Diying Yao, Marcelo Ehrlich, Yoav I Henis, Edward B Leof

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

63 citing papers in PubMed, 130 citations in OpenAlex.

  1. Article
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  6. Article
  7. Article
  8. Proactive and reactive roles of TGF-β in cancer.Seminars in cancer biology · 2023
    Review
  9. Review
  10. Article
  11. Article
  12. Transforming growth factor-β in tumour development.Frontiers in molecular biosciences · 2022
    Review
  13. Molecular Mechanisms of AMH Signaling.Frontiers in endocrinology · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

3 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

4 authors at 3 institutions in 2 countries.

Diying YaoDepartment of Biochemistry and Molecular Biology and Thoracic Diseases Research Unit, Mayo Clinic, Rochester, Minnesota 55905, USA.
Marcelo Ehrlich
Yoav I Henis
Edward B Leof
Tel Aviv University · ILMayo Clinic · USMayo Clinic in Florida · US

Funding

TGF BETA RECEPTORS AND CELL PROLIFERATIONR01GM054200 · NIGMS · MAYO CLINIC ROCHESTER · PI LEOF, EDWARD B · 1996 to 2018
$6.1M
TGF Beta Receptor DynamicsR37GM055816 · NIGMS · MAYO CLINIC ROCHESTER · PI LEOF, EDWARD B · 2009 to 2018
$3.6M
TGF BETA RECEPTOR DYNAMICSR01GM055816 · NIGMS · MAYO CLINIC ROCHESTER · PI LEOF, EDWARD B · 1997 to 2008
$2.4M
NIGMS NIH HHS GM-54200NIGMS NIH HHS GM-55816NIGMS NIH HHS R01 GM054200NIGMS NIH HHS R01 GM055816NIGMS NIH HHS R37 GM055816
6 · The paper itself

Abstract

Transforming growth factor-beta (TGF-beta) superfamily members regulate a wide range of biological processes by binding to two transmembrane serine/threonine kinase receptors, type I and type II. We have previously shown that the internalization of these receptors is inhibited by K(+) depletion, cytosol acidification, or hypertonic medium, suggesting the involvement of clathrin-coated pits. However, the involvement of the clathrin-associated adaptor complex AP2 and the identity of the AP2 subunit that binds the receptors were not known. Herein, we have studied these issues by combining studies on intact cells with in vitro assays. Using fluorescence photobleaching recovery to measure the lateral mobility of the receptors on live cells (untreated or treated to alter their coated pit structure), we demonstrated that their mobility is restricted by interactions with coated pits. These interactions were transient and mediated through the receptors' cytoplasmic tails. To measure direct binding of the receptors to specific AP2 subunits, we used yeast two-hybrid screens and in vitro biochemical assays. In contrast to most other plasma membrane receptors that bind to AP2 via the mu2 subunit, AP2/TGF-beta receptor binding was mediated by a direct interaction between the beta2-adaptin N-terminal trunk domain and the cytoplasmic tails of the receptors; no binding was observed to the mu2, alpha, or sigma2 subunits of AP2 or to mu1 of AP1. The data uniquely demonstrate both in vivo and in vitro the ability of beta2-adaptin to directly couple TGF-beta receptors to AP2 and to clathrin-coated pits, providing the first in vivo evidence for interactions of a transmembrane receptor with beta2-adaptin.

Indexed as

Adaptor Protein Complex 2Adaptor Protein Complex beta SubunitsAnimalsAntibodiesChlorpromazineClathrinCoated Pits, Cell-MembraneCOS CellsEndocytosisFluorescence Recovery After PhotobleachingProtein BindingProtein SubunitsReceptors, Transforming Growth Factor betaRecombinant Fusion ProteinsTwo-Hybrid System TechniquesAdaptor Protein Complex 2Adaptor Protein Complex beta SubunitsAntibodiesChlorpromazineClathrinProtein SubunitsReceptors, Transforming Growth Factor betaRecombinant Fusion Proteins

Identifiers

PMID12429842
PMCPMC133610
OpenAlexW2030360428

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.