Evidence map›Paper›PMID 20606011›Full record

ArticleMolecular and cellular biology2010

Independent and cooperative roles of adaptor molecules in proximal signaling during FcepsilonRI-mediated mast cell activation.

Taku Kambayashi, Mariko Okumura, Rebecca G Baker, Chih-Jung Hsu, Tobias Baumgart, Weiguo Zhang, Gary A Koretzky

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Immunoglobulin E receptor signaling and asthma.The Journal of biological chemistry · 2011
    Review
  10. Article
  11. Article
  12. Regulation of mast cell responses in health and disease.Critical reviews in immunology · 2011
    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

7 authors at 3 institutions in 1 country.

Taku KambayashiAbramson Family Cancer Research Institute, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6160, USA. taku.kambayashi@uphs.upenn.edu
Mariko Okumura
Rebecca G Baker
Chih-Jung Hsu
Tobias Baumgart
Weiguo Zhang
Gary A Koretzky
University of Pennsylvania · USCancer Research Institute · USDuke Medical Center · US

Funding

Analysis of adaptor protein (LAT) in TCR signalingR01AI048674 · NIAID · DUKE UNIVERSITY · PI ZHANG, WEIGUO · 2001 to 2011
$3.5M
TRANSFUSION MEDICINE RESEARCH TRAINING PROGRAMT32HL007775 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI SIEGEL, DONALD LAWRENCE · 1993 to 2023
$2.8M
Proximal signaling complexes in NK cell effector function and developmentR01HL107589 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI KAMBAYASHI, TAKU · 2011 to 2015
$2.0M
Adaptor molecules in lymphocyte signalingR01AI056156 · NIAID · DUKE UNIVERSITY · PI ZHANG, WEIGUO · 2003 to 2007
$1.5M
NHLBI NIH HHS R01 HL107589NHLBI NIH HHS T32 HL007775NIAID NIH HHS R01 AI048674NIAID NIH HHS R01 AI056156
6 · The paper itself

Abstract

Activation through FcepsilonRI, a high-affinity IgE-binding receptor, is critical for mast cell function during allergy. The formation of a multimolecular proximal signaling complex nucleated by the adaptor molecules SLP-76 and LAT1 is required for activation through this receptor. Based on previous T-cell studies, current dogma dictates that LAT1 is required for plasma membrane recruitment and function of SLP-76. Unexpectedly, we found that the recruitment and phosphorylation of SLP-76 were preserved in LAT1(-/-) mast cells and that SLP-76(-/-) and LAT1(-/-) mast cells harbored distinct functional and biochemical defects. The LAT1-like molecule LAT2 was responsible for the preserved membrane localization and phosphorylation of SLP-76 in LAT1(-/-) mast cells. Although LAT2 supported SLP-76 phosphorylation and recruitment to the plasma membrane, LAT2 only partially compensated for LAT1-mediated cell signaling due to its decreased ability to stabilize interactions with phospholipase Cgamma (PLCgamma). Comparison of SLP-76(-/-) LAT1(-/-) and SLP-76(-/-) mast cells revealed that some functions of LAT1 could occur independently of SLP-76. We propose that while SLP-76 and LAT1 depend on each other for many of their functions, LAT2/SLP-76 interactions and SLP-76-independent LAT1 functions also mediate a positive signaling pathway downstream of FcepsilonRI in mast cells.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid Transport System y+Amino Acid Transport System y+LAnimalsCalciumCells, CulturedFusion Regulatory Protein 1, Light ChainsGene DeletionMast CellsMicePhosphoproteinsPhosphorylationProtein TransportReceptors, IgEAdaptor Proteins, Signal TransducingAmino Acid Transport System y+Amino Acid Transport System y+LCalciumFusion Regulatory Protein 1, Light ChainsPhosphoproteinsReceptors, IgESlc7a7 protein, mouseSLC7A8 protein, mouseSLP-76 signal Transducing adaptor proteins

Identifiers

PMID20606011
PMCPMC2937553
OpenAlexW2165931997

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.