Evidence map›Paper›PMID 22496904›Full record

ArticlePloS one2012

NGF causes TrkA to specifically attract microtubules to lipid rafts.

Shona Pryor, Gretchen McCaffrey, Lindsay R Young, Mark L Grimes

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  7. Neurotrophic effects of GScientific reports · 2020
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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 2 institutions in 2 countries.

Shona PryorInstitute of Molecular Biosciences, Massey University, Palmerston North, New Zealand.
Gretchen McCaffrey
Lindsay R Young
Mark L Grimes
University of Montana · USMassey University · NZ

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 NIH NS070746-01NINDS NIH HHS NS061303-01NINDS NIH HHS R15 NS061303NINDS NIH HHS R15 NS070746OCPHP CDC HHS #PR-16455-02
6 · The paper itself

Abstract

Membrane protein sorting is mediated by interactions between proteins and lipids. One mechanism that contributes to sorting involves patches of lipids, termed lipid rafts, which are different from their surroundings in lipid and protein composition. Although the nerve growth factor (NGF) receptors, TrkA and p75(NTR) collaborate with each other at the plasma membrane to bind NGF, these two receptors are endocytosed separately and activate different cellular responses. We hypothesized that receptor localization in membrane rafts may play a role in endocytic sorting. TrkA and p75(NTR) both reside in detergent-resistant membranes (DRMs), yet they responded differently to a variety of conditions. The ganglioside, GM1, caused increased association of NGF, TrkA, and microtubules with DRMs, but a decrease in p75(NTR). When microtubules were induced to polymerize and attach to DRMs by in vitro reactions, TrkA, but not p75(NTR), was bound to microtubules in DRMs and in a detergent-resistant endosomal fraction. NGF enhanced the interaction between TrkA and microtubules in DRMs, yet tyrosine phosphorylated TrkA was entirely absent in DRMs under conditions where activated TrkA was detected in detergent-sensitive membranes and endosomes. These data indicate that TrkA and p75(NTR) partition into membrane rafts by different mechanisms, and that the fraction of TrkA that associates with DRMs is internalized but does not directly form signaling endosomes. Rather, by attracting microtubules to lipid rafts, TrkA may mediate other processes such as axon guidance.

Indexed as

AnimalsEndosomesG(M1) GangliosideMembrane MicrodomainsMicrotubulesNerve Growth FactorNerve Tissue ProteinsPC12 CellsRatsReceptors, Growth FactorReceptor, trkASignal TransductionG(M1) GangliosideNerve Growth FactorNerve Tissue ProteinsNgfr protein, ratReceptors, Growth FactorReceptor, trkA

Identifiers

PMID22496904
PMCPMC3319630
OpenAlexW1977621980

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.