Evidence map›Paper›PMID 20308635›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2010

Functional analysis of Lyn kinase A and B isoforms reveals redundant and distinct roles in Fc epsilon RI-dependent mast cell activation.

Damiana Alvarez-Errico, Yumi Yamashita, Ryo Suzuki, Sandra Odom, Yasuko Furumoto, Toshiyuki Yamashita, Juan Rivera

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Get Spliced: Uniting Alternative Splicing and Arthritis.International journal of molecular sciences · 2024
    Review
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  5. Article
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  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Functions of the Lyn tyrosine kinase in health and disease.Cell communication and signaling : CCS · 2012
    Article
  20. Lyn but not Fyn kinase controls IgG-mediated systemic anaphylaxis.Journal of immunology (Baltimore, Md. : 1950) · 2012
    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

7 authors at 2 institutions in 2 countries.

Damiana Alvarez-ErricoLaboratory of Molecular Immunogenetics, Department of Health and Human Services, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Yumi Yamashita
Ryo Suzuki
Sandra Odom
Yasuko Furumoto
Toshiyuki Yamashita
Juan Rivera
National Institutes of Health · USNational Institute of Arthritis and Musculoskeletal and Skin Diseases · US

Funding

NIAMS Light Imaging FacilityZICAR041186 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI RANDAZZO, DAVIDE · 2010 to 2025
$18.2M
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
Intramural NIH HHS ZIA AR041101
6 · The paper itself

Abstract

Engagement of FcepsilonRI causes its phosphorylation by Lyn kinase. Two alternatively spliced variants, Lyn A and B, are expressed in mast cells, and both isoforms interact with FcepsilonRI. Unlike Lyn A, Lyn B lacks a 21-aa region in the N-terminal unique domain. In this study, we investigated the role of Lyn A and B isoforms in mast cell signaling and responses. Lyn B was found to be a poor inducer of mast cell degranulation and was less potent in both inositol 1,4,5-triphosphate production and calcium responses. Expression of Lyn B alone showed reduced phosphorylation of both phospholipase Cgamma-1 and -2 and decreased interaction of phospholipase Cgamma-1 with the phosphorylated linker for activation of T cells. Lyn B also showed increased binding of tyrosine-phosphorylated proteins, which included the negative regulatory lipid phosphatase SHIP-1. In contrast, both Lyn A and B caused similar total cellular tyrosine phosphorylation and FcepsilonRI phosphorylation and neither Lyn A nor Lyn B alone could completely restore mast cell degranulation or dampen the excessive cytokine production seen in the absence of Lyn. However, expression of both isoforms showed complementation and normalized responses. These findings demonstrate that Lyn B differs from Lyn A in its association with SHIP-1 and in the regulation of calcium responses. However, complementation of both isoforms is required in mast cell activation.

Indexed as

AnimalsCalciumCalcium SignalingCell DegranulationCell LineCells, CulturedEnzyme ActivationFemaleHumansInositol Polyphosphate 5-PhosphatasesIntracellular Signaling Peptides and ProteinsIsoenzymesMast CellsMiceMice, Inbred C57BLMice, KnockoutCalciumInositol Polyphosphate 5-PhosphatasesINPP5D protein, humanInpp5d protein, mouseIntracellular Signaling Peptides and ProteinsIsoenzymeslyn protein-tyrosine kinasePhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphoric Monoester HydrolasesProtein-Tyrosine KinasesReceptors, IgEsrc-Family KinasesSyk KinaseSYK protein, humanSyk protein, mouse

Identifiers

PMID20308635
PMCPMC2948211
OpenAlexW2165073961

What OpenQuestion holds

Textmetadata
LicenceTDM
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.