Evidence map›Paper›PMID 19427382›Full record

ArticleJournal of structural biology2009

Roles for SH2 and SH3 domains in Lyn kinase association with activated FcepsilonRI in RBL mast cells revealed by patterned surface analysis.

Stephanie Hammond, Alice Wagenknecht-Wiesner, Sarah L Veatch, David Holowka, Barbara Baird

Open access · greenAbstract read
In one paragraph

Article in Journal of structural biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

9 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Article
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  4. 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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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

5 authors at 1 institution in 1 country.

Stephanie HammondDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA.
Alice Wagenknecht-Wiesner
Sarah L Veatch
David Holowka
Barbara Baird
Cornell University · US

Funding

STUCTURE-FUNCTION RELATIONSHIPS OF IMMUNORECEPTORSR01AI018306 · NIAID · CORNELL UNIVERSITY ITHACA · PI BAIRD, BARBARA A · 1985 to 2014
$5.3M
BIOPHYSICAL AND BIOCHEMICAL PHARMACOLOGYT32GM008210 · NIGMS · CORNELL UNIVERSITY ITHACA · PI SHARP, GEOFFREY W · 1988 to 2007
$1.3M
Mechanistic studies of membrane lateral organization in cell plasma membranes.K99GM087810 · NIGMS · CORNELL UNIVERSITY · PI VEATCH, SARAH L · 2009 to 2010
$127k
NIAID NIH HHS R01 AI018306NIAID NIH HHS R01-AI018306NIGMS NIH HHS K99 GM087810NIGMS NIH HHS T32 GM008210NIGMS NIH HHS T32-GM08210
6 · The paper itself

Abstract

In mast cells, antigen-mediated cross-linking of IgE bound to its high-affinity surface receptor, FcepsilonRI, initiates a signaling cascade that culminates in degranulation and release of allergic mediators. Antigen-patterned surfaces, in which the antigen is deposited in micron-sized features on a silicon substrate, were used to examine the spatial relationship between clustered IgE-FcepsilonRI complexes and Lyn, the signal-initiating tyrosine kinase. RBL mast cells expressing wild-type Lyn-EGFP showed co-redistribution of this protein with clustered IgE receptors on antigen-patterned surfaces, whereas Lyn-EGFP containing an inhibitory point mutation in its SH2 domain did not significantly accumulate with the patterned antigen, and Lyn-EGFP with an inhibitory point mutation in its SH3 domain exhibited reduced interactions. Our results using antigen-patterned surfaces and quantitative cross-correlation image analysis reveal that both the SH2 and SH3 domains contribute to interactions between Lyn kinase and cross-linked IgE receptors in stimulated mast cells.

Indexed as

AnimalsMast CellsMicePoint MutationProtein BindingReceptors, IgEsrc-Family Kinasessrc Homology Domainslyn protein-tyrosine kinaseReceptors, IgEsrc-Family Kinases

Identifiers

PMID19427382
PMCPMC2767321
OpenAlexW2004469343

What OpenQuestion holds

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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.