Evidence map›Paper›PMID 16275755›Full record

ArticleThe Journal of cell biology2005

Temporally resolved interactions between antigen-stimulated IgE receptors and Lyn kinase on living cells.

Daniel R Larson, Julie A Gosse, David A Holowka, Barbara A Baird, Watt W Webb

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
10.8field-weighted citation impact, top 1% 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

58 citing papers in PubMed, 117 citations in OpenAlex.

  1. Review
  2. 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
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Correcting for spectral cross-talk in dual-color fluorescence cross-correlation spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2012
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Daniel R LarsonSchool of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853, USA.
Julie A Gosse
David A Holowka
Barbara A Baird
Watt W Webb
Cornell University · US

Funding

Biotechnology Resource Digital Electro-Optical ImagingP41EB001976 · NIBIB · CORNELL UNIVERSITY ITHACA · PI ZIPFEL, WARREN R · 2003 to 2010
$6.9M
STUCTURE-FUNCTION RELATIONSHIPS OF IMMUNORECEPTORSR01AI018306 · NIAID · CORNELL UNIVERSITY ITHACA · PI BAIRD, BARBARA A · 1985 to 2014
$5.3M
NIAID NIH HHS AI18306NIAID NIH HHS R01 AI018306NIBIB NIH HHS 9 P41 EB001976NIBIB NIH HHS P41 EB001976
6 · The paper itself

Abstract

Upon cross-linking by antigen, the high affinity receptor for immunoglobulin E (IgE), FcepsilonRI, is phosphorylated by the Src family tyrosine kinase Lyn to initiate mast cell signaling, leading to degranulation. Using fluorescence correlation spectroscopy (FCS), we observe stimulation-dependent associations between fluorescently labeled IgE-FcepsilonRI and Lyn-EGFP on individual cells. We also simultaneously measure temporal variations in the lateral diffusion of these proteins. Antigen-stimulated interactions between these proteins detected subsequent to the initiation of receptor phosphorylation exhibit time-dependent changes, suggesting multiple associations between FcepsilonRI and Lyn-EGFP. During this period, we also observe a persistent decrease in Lyn-EGFP lateral diffusion that is dependent on Src family kinase activity. These stimulated interactions are not observed between FcepsilonRI and a chimeric EGFP that contains only the membrane-targeting sequence from Lyn. Our results reveal real-time interactions between Lyn and cross-linked FcepsilonRI implicated in downstream signaling events. They demonstrate the capacity of FCS cross-correlation analysis to investigate the mechanism of signaling-dependent protein-protein interactions in intact, living cells.

Indexed as

AnimalsCell DegranulationCell LineCell MembraneDiffusionGreen Fluorescent ProteinsHumansImmunoglobulin EMast CellsMembrane MicrodomainsMicePhosphorylationRatsReceptors, IgERecombinant Fusion ProteinsSignal Transductionenhanced green fluorescent proteinGreen Fluorescent ProteinsImmunoglobulin Elyn protein-tyrosine kinaseReceptors, IgERecombinant Fusion Proteinssrc-Family Kinases

Identifiers

PMID16275755
PMCPMC2171255
OpenAlexW1969399881

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.