Evidence map›Paper›PMID 25343439›Full record

ArticleACS chemical biology2015

Fluorogen-activating proteins provide tunable labeling densities for tracking FcεRI independent of IgE.

Samantha L Schwartz, Qi Yan, Cheryl A Telmer, Keith A Lidke, Marcel P Bruchez, Diane S Lidke

Abstract read
In one paragraph

Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.8field-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

24 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Genetically Encoded Activators of Small Molecules for Imaging and Drug Delivery.Angewandte Chemie (International ed. in English) · 2020
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Fluorogenic Labeling Strategies for Biological Imaging.International journal of molecular sciences · 2017
    Review
  16. Review
  17. Article
  18. Article
  19. Small fluorescence-activating and absorption-shifting tag for tunable protein imaging in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  20. 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

6 authors at 3 institutions in 1 country.

Samantha L SchwartzDepartment of Pathology and Cancer Research and Treatment Center, ‡Department of Physics and Astronomy, University of New Mexico , Albuquerque, New Mexico 87131, United States.
Qi Yan
Cheryl A Telmer
Keith A Lidke
Marcel P Bruchez
Diane S Lidke
University of New Mexico · USCarnegie Mellon University · USImaging Center · US

Funding

WOMEN'S CANCERS RESEARCH PROGRAMP30CA118100 · NCI · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI Yolanda Sanchez · 2005 to 2026
$57.1M
Fluorescent Biosensors for Networks and PathwaysU54GM103529 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI WAGGONER, ALAN S. · 2012 to 2013
$6.3M
Single Molecule Imaging to Quantify FcεRI Signaling DynamicsR01GM100114 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI LIDKE, DIANE · 2012 to 2016
$1.4M
NCI NIH HHS P30 CA118100NIGMS NIH HHS 8U54GM103529NIGMS NIH HHS P50GM0852673NIGMS NIH HHS R01 GM100114NIGMS NIH HHS R01GM100114NIGMS NIH HHS U54 GM103529
6 · The paper itself

Abstract

Crosslinking of IgE bound FcεRI on mast cells and basophils by multivalent antigen leads to degranulation and the release of key inflammatory mediators that stimulate the allergic response. Here, we present and characterize the use of fluorogen-activating proteins (FAPs) for single particle tracking of FcεRI to investigate how receptor mobility is influenced after IgE-induced changes in mast cell behavior. FAPs are genetically encoded tags that bind a fluorogen dye and increase its brightness upon binding up to 20,000-fold. We demonstrate that, by titrating fluorogen concentration, labeling densities from ensemble to single particle can be achieved, independent of expression level and without the need for wash steps or photobleaching. The FcεRI γ-subunit fused to a FAP (FAP-γ) provides, for the first time, an IgE-independent probe for tracking this signaling subunit of FcεRI at the single molecule level. We show that the FcεRI γ-subunit dynamics are controlled by the IgE-binding α-subunit and that the cytokinergic IgE, SPE-7, induces mast cell activation without altering FcεRI mobility or promoting internalization. We take advantage of the far-red emission of the malachite green (MG) fluorogen to track FcεRI relative to dynamin-GFP and find that immobilized receptors readily correlate with locations of dynamin recruitment only under conditions that promote rapid endocytosis. These studies demonstrate the usefulness of the FAP system for single molecule studies and have provided new insights into the relationship among FcεRI structure, activity, and mobility.

Indexed as

AnimalsCell LineFlow CytometryImmunoglobulin EMicrotubule-Associated ProteinsProteinsProtein Serine-Threonine KinasesRatsReceptors, IgESignal TransductionImmunoglobulin EMicrotubule-Associated ProteinsMtssk protein, mouseProteinsProtein Serine-Threonine KinasesReceptors, IgE

Identifiers

PMID25343439
PMCPMC4340345
OpenAlexW2313335569

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.