Evidence map›Paper›PMID 27875277›Full record

ArticleJournal of cell science2016

Development of nanoscale structure in LAT-based signaling complexes.

Valarie A Barr, Eilon Sherman, Jason Yi, Itoro Akpan, Alexandre K Rouquette-Jazdanian, Lawrence E Samelson

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Heterogeneity of Signaling Complex Nanostructure in T Cells Activated Via the T Cell Antigen Receptor.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Microclusters as T Cell Signaling Hubs: Structure, Kinetics, and Regulation.Frontiers in cell and developmental biology · 2020
    Review
  10. Article
  11. Review
  12. Article
  13. 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 1 institution in 1 country.

Valarie A BarrLaboratory of Cellular and Molecular Biology, CCR, NCI, NIH, Bethesda, MD 20892, USA.ORCID 0000-0001-5377-4753
Eilon ShermanRacah Institute of Physics, The Hebrew University, Jerusalem 91904, Israel.ORCID 0000-0002-7403-6036
Jason YiLaboratory of Cellular and Molecular Biology, CCR, NCI, NIH, Bethesda, MD 20892, USA.ORCID 0000-0001-5131-6767
Itoro AkpanLaboratory of Cellular and Molecular Biology, CCR, NCI, NIH, Bethesda, MD 20892, USA.ORCID 0000-0002-3239-6252
Alexandre K Rouquette-JazdanianLaboratory of Cellular and Molecular Biology, CCR, NCI, NIH, Bethesda, MD 20892, USA.ORCID 0000-0003-2646-0040
Lawrence E SamelsonLaboratory of Cellular and Molecular Biology, CCR, NCI, NIH, Bethesda, MD 20892, USA samelsonl@helix.nih.gov.ORCID 0000-0002-5963-2112
Hebrew University of Jerusalem · IL

Funding

Confocal Core for the Laboratory of Cellular and Molecular BiologyZICBC010978 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI PALLIKKUTH, SANDEEP · 2009 to 2025
$7.6M
6 · The paper itself

Abstract

The adapter molecule linker for activation of T cells (LAT) plays a crucial role in forming signaling complexes induced by stimulation of the T cell receptor (TCR). These multi-molecular complexes are dynamic structures that activate highly regulated signaling pathways. Previously, we have demonstrated nanoscale structure in LAT-based complexes where the adapter SLP-76 (also known as LCP2) localizes to the periphery of LAT clusters. In this study, we show that initially LAT and SLP-76 are randomly dispersed throughout the clusters that form upon TCR engagement. The segregation of LAT and SLP-76 develops near the end of the spreading process. The local concentration of LAT also increases at the same time. Both changes require TCR activation and an intact actin cytoskeleton. These results demonstrate that the nanoscale organization of LAT-based signaling complexes is dynamic and indicates that different kinds of LAT-based complexes appear at different times during T cell activation.

Indexed as

Signal TransductionActin CytoskeletonAdaptor Proteins, Signal TransducingGreen Fluorescent ProteinsHumansJurkat CellsLymphocyte ActivationMembrane FluidityMembrane ProteinsMicroscopyNanostructuresPhosphoproteinsReceptors, Antigen, T-CellAdaptor Proteins, Signal TransducingGreen Fluorescent ProteinsLAT protein, humanMembrane ProteinsPhosphoproteinsReceptors, Antigen, T-CellSLP-76 signal Transducing adaptor proteinsMicroclusterNanostructurePhotoactivated localization microscopySignaling complexSingle-molecule localization microscopyT cell activation

Identifiers

PMID27875277
PMCPMC5201021
OpenAlexW2551477566

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.