Evidence map›Paper›PMID 11713268›Full record

ArticleMolecular and cellular biology2001

Structure-function analysis of Lyn kinase association with lipid rafts and initiation of early signaling events after Fcepsilon receptor I aggregation.

M Kovárová, P Tolar, R Arudchandran, L Dráberová, J Rivera, P Dráber

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
4.5field-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

90 citing papers in PubMed, 177 citations in OpenAlex.

  1. Toll like receptor 4 (TLR4) in neuroinflammation: From acute hemorrhagic stroke to chronic neurodegeneration.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2026
    Review
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  10. Lipid-based and protein-based interactions synergize transmembrane signaling stimulated by antigen clustering of IgE receptors.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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  14. Review
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  20. Proteomic Analysis of Lipid Rafts from RBL-2H3 Mast Cells.International journal of molecular sciences · 2019
    Article

30 more citing papers are in PubMed but not listed here.

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 4 institutions in 2 countries.

M KovárováInstitute of Molecular Genetics, Academy of Sciences of the Czech Republic, 14220 Prague, Czech Republic.
P Tolar
R Arudchandran
L Dráberová
J Rivera
P Dráber
Czech Academy of Sciences, Institute of Molecular Genetics · CZNational Institute of Arthritis and Musculoskeletal and Skin Diseases · USCzech Academy of Sciences · CZNational Institutes of Health · US

Funding

Intracellular Signaling By The Cell Surface Receptor For IgEZIAAR041101 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI RIVERA, JUAN · 2009 to 2013
$4.8M
INTRACELLULAR SIGNALING BY THE CELL SURFACE RECEPTOR FOR IGEZ01AR041101 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI RIVERA, JUAN · 1995 to 2008
$2.7M
6 · The paper itself

Abstract

The first step in immunoreceptor signaling is represented by ligand-dependent receptor aggregation, followed by receptor phosphorylation mediated by tyrosine kinases of the Src family. Recently, sphingolipid- and cholesterol-rich plasma membrane microdomains, called lipid rafts, have been identified and proposed to function as platforms where signal transduction molecules may interact with the aggregated immunoreceptors. Here we show that aggregation of the receptors with high affinity for immunoglobulin E (FcepsilonRI) in mast cells is accompanied by a co-redistribution of the Src family kinase Lyn. The co-redistribution requires Lyn dual fatty acylation, Src homology 2 (SH2) and/or SH3 domains, and Lyn kinase activity, in cis or in trans. Palmitoylation site-mutated Lyn, which is anchored to the plasma membrane but exhibits reduced sublocalization into lipid rafts, initiates the tyrosine phosphorylation of FcepsilonRI subunits, Syk protein tyrosine kinase, and the linker for activation of T cells, along with an increase in the concentration of intracellular Ca(2+). However, Lyn mutated in both the palmitoylation and myristoylation sites does not anchor to the plasma membrane and is incapable of initiating FcepsilonRI phosphorylation and early signaling events. These data, together with our finding that a constitutively tyrosine-phosphorylated FcepsilonRI does not exhibit an increased association with lipid rafts, suggest that FcepsilonRI phosphorylation and early activation events can be initiated outside of lipid rafts.

Indexed as

AnimalsAntigensCalciumCell MembraneCholesterolDetergentsDNADNA FragmentationEnzyme ActivationGreen Fluorescent ProteinsImmunoblottingLipid MetabolismLuminescent ProteinsMembrane MicrodomainsMiceMicroscopy, ConfocalAntigensCalciumCholesterolDetergentsDNAGreen Fluorescent ProteinsLuminescent Proteinslyn protein-tyrosine kinaseMyristic AcidOctoxynolPalmitic AcidPhosphotyrosineReceptors, IgERecombinant ProteinsSphingolipidssrc-Family KinasesTyrosine

Identifiers

PMID11713268
PMCPMC99996
OpenAlexW2147482146

What OpenQuestion holds

Textmetadata
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.