Evidence map›Paper›PMID 17634290›Full record

ArticleMolecular biology of the cell2007

A unique element in the cytoplasmic tail of the type II transforming growth factor-beta receptor controls basolateral delivery.

Stephen J Murphy, Keren E Shapira, Yoav I Henis, Edward B Leof

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Signaling Receptors for TGF-β Family Members.Cold Spring Harbor perspectives in biology · 2016
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. 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

4 authors.

Stephen J MurphyThoracic Diseases Research Unit, Department of Biochemistry and Molecular Biology and Mayo Clinic Cancer Center, Mayo Clinic College of Medicine, Rochester, MN 55905, USA.
Keren E Shapira
Yoav I Henis
Edward B Leof

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 (TGF)-beta receptors stimulate diverse signaling processes that control a wide range of biological responses. In polarized epithelia, the TGFbeta type II receptor (T2R) is localized at the basolateral membranes. Sequential cytoplasmic truncations resulted in receptor missorting to apical surfaces, and they indicated an essential targeting element(s) near the receptor's C terminus. Point mutations in the full-length receptor confirmed this prediction, and a unique basolateral-targeting region was elucidated between residues 529 and 538 (LTAxxVAxxR) that was distinct, but colocalized within a clinically significant signaling domain essential for TGFbeta-dependent activation of the Smad2/3 cascade. Transfer of a terminal 84 amino-acid fragment, containing the LTAxxVAxxR element, to the apically sorted influenza hemagglutinin (HA) protein was dominant and directed basolateral HA expression. Although delivery to the basolateral surfaces was direct and independent of any detectable transient apical localization, fluorescence recovery after photobleaching demonstrated similar mobility for the wild-type receptor and a missorted mutant lacking the targeting motif. This latter finding excludes the possibility that the domain acts as a cell membrane retention signal, and it supports the hypothesis that T2R sorting occurs from an intracellular compartment.

Indexed as

Cell PolarityAmino Acid MotifsAmino AcidsAnimalsBiotinylationChlorocebus aethiopsCOS CellsCytoplasmDogsHeLa CellsHemagglutininsHumansProtein Serine-Threonine KinasesProtein Sorting SignalsProtein Structure, TertiaryProtein TransportAmino AcidsHemagglutininsProtein Serine-Threonine KinasesProtein Sorting SignalsReceptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type IReceptor, Transforming Growth Factor-beta Type IIRecombinant Fusion ProteinsViral Proteins

Identifiers

PMID17634290
PMCPMC1995729

What OpenQuestion holds

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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.