Evidence map›Paper›PMID 25884760›Full record

ArticlePLoS computational biology2015

Neuroblastoma tyrosine kinase signaling networks involve FYN and LYN in endosomes and lipid rafts.

Juan Palacios-Moreno, Lauren Foltz, Ailan Guo, Matthew P Stokes, Emily D Kuehn, Lynn George, Michael Comb, Mark L Grimes

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed, 1 pooled it
4.9field-weighted citation impact, top 5% 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

48 citing papers in PubMed, 1 synthesis or guideline pooled it, 73 citations in OpenAlex.

  1. Pooled it
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  12. Pharmacological Inhibition of PTEN Rescues Dopaminergic Neurons by Attenuating Apoptotic and Neuroinflammatory Signaling Events.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2023
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  19. Article
  20. Regulatory effects of post-translational modifications on zDHHCThe Journal of biological chemistry · 2020
    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

8 authors at 4 institutions in 1 country.

Juan Palacios-MorenoDivision of Biological Sciences, Center for Structural and Functional Neuroscience, University of Montana, Missoula, Montana, United States of America.
Lauren FoltzDivision of Biological Sciences, Center for Structural and Functional Neuroscience, University of Montana, Missoula, Montana, United States of America.
Ailan GuoCell Signaling Technology, Inc., Danvers, Massachusetts, United States of America.
Matthew P StokesCell Signaling Technology, Inc., Danvers, Massachusetts, United States of America.
Emily D KuehnDepartment of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States of America.
Lynn GeorgeDepartment of Cell Biology and Neuroscience, Montana State University, Bozeman, Montana, United States of America.
Michael CombCell Signaling Technology, Inc., Danvers, Massachusetts, United States of America.
Mark L GrimesDivision of Biological Sciences, Center for Structural and Functional Neuroscience, University of Montana, Missoula, Montana, United States of America.
Cell Signaling Technology (United States) · USUniversity of Montana · USJohns Hopkins Medicine · USMontana State University · US

Funding

Understanding the molecular mechanism of pathogenesis of prion diseasesP20RR015583 · NCRR · UNIVERSITY OF MONTANA · PI KAVANAUGH, MICHAEL PATRICK · 2000 to 2009
$17.6M
Receptor Tyrosine Kinase Sorting and Transactivation in EndosomesR15NS070746 · NINDS · UNIVERSITY OF MONTANA · PI GRIMES, MARK LINDSAY · 2010 to 2010
$422k
Membrane Traffic Sorting Mechanisms That Produce TrkA Signaling EndosomesR15NS061303 · NINDS · UNIVERSITY OF MONTANA · PI GRIMES, MARK LINDSAY · 2008 to 2008
$212k
NCRR NIH HHS P20 RR015583NINDS NIH HHS NS061303-01NINDS NIH HHS NS070746-01NINDS NIH HHS R15 NS061303NINDS NIH HHS R15 NS070746
6 · The paper itself

Abstract

Protein phosphorylation plays a central role in creating a highly dynamic network of interacting proteins that reads and responds to signals from growth factors in the cellular microenvironment. Cells of the neural crest employ multiple signaling mechanisms to control migration and differentiation during development. It is known that defects in these mechanisms cause neuroblastoma, but how multiple signaling pathways interact to govern cell behavior is unknown. In a phosphoproteomic study of neuroblastoma cell lines and cell fractions, including endosomes and detergent-resistant membranes, 1622 phosphorylated proteins were detected, including more than half of the receptor tyrosine kinases in the human genome. Data were analyzed using a combination of graph theory and pattern recognition techniques that resolve data structure into networks that incorporate statistical relationships and protein-protein interaction data. Clusters of proteins in these networks are indicative of functional signaling pathways. The analysis indicates that receptor tyrosine kinases are functionally compartmentalized into distinct collaborative groups distinguished by activation and intracellular localization of SRC-family kinases, especially FYN and LYN. Changes in intracellular localization of activated FYN and LYN were observed in response to stimulation of the receptor tyrosine kinases, ALK and KIT. The results suggest a mechanism to distinguish signaling responses to activation of different receptors, or combinations of receptors, that govern the behavior of the neural crest, which gives rise to neuroblastoma.

Indexed as

Signal TransductionAdaptor Proteins, Signal TransducingCell Line, TumorComputer SimulationEndosomesHumansMembrane MicrodomainsModels, BiologicalNeoplasm ProteinsNeuroblastomaPhosphoproteinsProtein-Tyrosine Kinasessrc-Family KinasesAdaptor Proteins, Signal TransducingFYB1 protein, humanlyn protein-tyrosine kinaseNeoplasm ProteinsPhosphoproteinsProtein-Tyrosine Kinasessrc-Family Kinases

Identifiers

PMID25884760
PMCPMC4401789
OpenAlexW2056017011

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.