Evidence map›Paper›PMID 26337383›Full record

ArticleMolecular biology of the cell2015

Sorting nexin 9 differentiates ligand-activated Smad3 from Smad2 for nuclear import and transforming growth factor β signaling.

Mark C Wilkes, Claire E Repellin, Jeong-Han Kang, Mahefatiana Andrianifahanana, Xueqian Yin, Edward B Leof

Open access · greenAbstract 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 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Review
  3. The emerging role of sorting nexins in cardiovascular diseases.Clinical science (London, England : 1979) · 2019
    Review
  4. Article
  5. 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

6 authors at 2 institutions in 2 countries.

Mark C WilkesThoracic Diseases Research Unit, Department of Pulmonary and Critical Care Medicine, Mayo Clinic College of Medicine, Rochester, MN 55905.
Claire E RepellinThoracic Diseases Research Unit, Department of Pulmonary and Critical Care Medicine, Mayo Clinic College of Medicine, Rochester, MN 55905.
Jeong-Han KangThoracic Diseases Research Unit, Department of Pulmonary and Critical Care Medicine, Mayo Clinic College of Medicine, Rochester, MN 55905.
Mahefatiana AndrianifahananaThoracic Diseases Research Unit, Department of Pulmonary and Critical Care Medicine, Mayo Clinic College of Medicine, Rochester, MN 55905.
Xueqian YinThoracic Diseases Research Unit, Department of Pulmonary and Critical Care Medicine, Mayo Clinic College of Medicine, Rochester, MN 55905.
Edward B LeofThoracic Diseases Research Unit, Department of Pulmonary and Critical Care Medicine, Mayo Clinic College of Medicine, Rochester, MN 55905 leof.edward@mayo.edu.
Mayo Clinic · USUniversity of California, Berkeley · 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 β (TGFβ) is a pleiotropic protein secreted from essentially all cell types and primary tissues. While TGFβ's actions reflect the activity of a number of signaling networks, the primary mediator of TGFβ responses are the Smad proteins. Following receptor activation, these cytoplasmic proteins form hetero-oligomeric complexes that translocate to the nucleus and affect gene transcription. Here, through biological, biochemical, and immunofluorescence approaches, sorting nexin 9 (SNX9) is identified as being required for Smad3-dependent responses. SNX9 interacts with phosphorylated (p) Smad3 independent of Smad2 or Smad4 and promotes more rapid nuclear delivery than that observed independent of ligand. Although SNX9 does not bind nucleoporins Nup153 or Nup214 or some β importins (Imp7 or Impβ), it mediates the association of pSmad3 with Imp8 and the nuclear membrane. This facilitates nuclear translocation of pSmad3 but not SNX9.

Indexed as

Active Transport, Cell NucleusAnimalsCell Culture TechniquesCell NucleusHumansKaryopherinsLigandsMiceNuclear Pore Complex ProteinsPhosphorylationProtein BindingProtein TransportSignal TransductionSmad2 ProteinSmad3 ProteinSmad4 ProteinKaryopherinsLigandsNuclear Pore Complex ProteinsSmad2 ProteinSMAD2 protein, humanSmad3 ProteinSmad4 ProteinSmad ProteinsSNX9 protein, humanSorting NexinsTrans-ActivatorsTransforming Growth Factor beta

Identifiers

PMID26337383
PMCPMC4626071
OpenAlexW2311995955

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.