Evidence map›Paper›PMID 25888394›Full record

ArticleBMC biochemistry2015

Solution structure and biophysical characterization of the multifaceted signalling effector protein growth arrest specific-1.

Katja Rosti, Adrian Goldman, Tommi Kajander

Open access · hybridAbstract read
In one paragraph

Article in BMC biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Gas1-Mediated Suppression of Hepatoblastoma Tumorigenesis.The American journal of pathology · 2025
    Article
  3. Article
  4. Article
  5. Pre- and postnatal exposure of mice to concentrated urban PMEnvironmental pollution (Barking, Essex : 1987) · 2018
    Article
  6. 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

3 authors at 2 institutions in 2 countries.

Katja RostiInstitute of Biotechnology, Structural Biology and Biophysics, University of Helsinki, Helsinki, Finland. katja.rosti@helsinki.fi.
Adrian GoldmanAstbury Centre for Structural Molecular Biology, School of Biomedical Sciences, University of Leeds, Leeds, UK. a.goldman@leeds.ac.uk.
Tommi KajanderInstitute of Biotechnology, Structural Biology and Biophysics, University of Helsinki, Helsinki, Finland. tommi.kajander@helsinki.fi.
University of Helsinki · FIUniversity of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe protein growth arrest specific-1 (GAS1) was discovered based on its ability to stop the cell cycle. During development it is involved in embryonic patterning, inhibits cell proliferation and mediates cell death, and has therefore been considered as a tumor suppressor. GAS1 is known to signal through two different cell membrane receptors: Rearranged during transformation (RET), and the sonic hedgehog receptor Patched-1. Sonic Hedgehog signalling is important in stem cell renewal and RET mediated signalling in neuronal survival. Disorders in both sonic hedgehog and RET signalling are connected to cancer progression. The neuroprotective effect of RET is controlled by glial cell-derived neurotrophic factor family ligands and glial cell-derived neurotrophic factor receptor alphas (GFRαs). Human Growth arrest specific-1 is a distant homolog of the GFRαs.

resultsWe have produced and purified recombinant human GAS1 protein, and confirmed that GAS1 is a monomer in solution by static light scattering and small angle X-ray scattering analysis. The low resolution solution structure reveals that GAS1 is more elongated and flexible than the GFRαs, and the homology modelling of the individual domains show that they differ from GFRαs by lacking the amino acids for neurotrophic factor binding. In addition, GAS1 has an extended loop in the N-terminal domain that is conserved in vertebrates after the divergence of fishes and amphibians.

conclusionsWe conclude that GAS1 most likely differs from GFRαs functionally, based on comparative structural analysis, while it is able to bind the extracellular part of RET in a neurotrophic factor independent manner, although with low affinity in solution. Our structural characterization indicates that GAS1 differs from GFRα's significantly also in its conformation, which probably reflects the functional differences between GAS1 and the GFRαs.

Indexed as

Biophysical PhenomenaAmino Acid SequenceAnimalsCell Cycle ProteinsCell LineEvolution, MolecularGlial Cell Line-Derived Neurotrophic FactorGPI-Linked ProteinsHumansModels, MolecularMolecular Sequence DataProtein StabilityProtein Structure, TertiarySequence AnalysisSequence Homology, Amino AcidSolutionsCell Cycle ProteinsGAS1 protein, humanGlial Cell Line-Derived Neurotrophic FactorGPI-Linked ProteinsSolutions

Identifiers

PMID25888394
PMCPMC4349606
OpenAlexW2012535427

What OpenQuestion holds

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LicenceCC BY
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.