Evidence map›Paper›PMID 26354432›Full record

ReviewThe Journal of biological chemistry2015

The linker for activation of T cells (LAT) signaling hub: from signaling complexes to microclusters.

Lakshmi Balagopalan, Robert L Kortum, Nathan P Coussens, Valarie A Barr, Lawrence E Samelson

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

96 citing papers in PubMed, 137 citations in OpenAlex.

  1. LAT condensation gates PLCγ1 activation via bimodal LAT phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  13. Parallel reactions on a single T cell receptor offer a robust kinetic proofreading mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2025
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36 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 1 country.

Lakshmi BalagopalanFrom the Laboratory of Cellular and Molecular Biology, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 20892-4256.
Robert L Kortumthe Department of Pharmacology, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814, and.
Nathan P Coussensthe Division of Pre-Clinical Innovation, National Center for Advancing Translational Sciences, National Institutes of Health, Rockville, Maryland 20850.
Valarie A BarrFrom the Laboratory of Cellular and Molecular Biology, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 20892-4256.
Lawrence E SamelsonFrom the Laboratory of Cellular and Molecular Biology, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 20892-4256, samelsonl@helix.nih.gov.
National Institutes of Health · USNational Center for Advancing Translational Sciences · USUniformed Services University of the Health Sciences · US

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
Intramural NIH HHS
6 · The paper itself

Abstract

Since the cloning of the critical adapter, LAT (linker for activation of T cells), more than 15 years ago, a combination of multiple scientific approaches and techniques continues to provide valuable insights into the formation, composition, regulation, dynamics, and function of LAT-based signaling complexes. In this review, we will summarize current views on the assembly of signaling complexes nucleated by LAT. LAT forms numerous interactions with other signaling molecules, leading to cooperativity in the system. Furthermore, oligomerization of LAT by adapter complexes enhances intracellular signaling and is physiologically relevant. These results will be related to data from super-resolution microscopy studies that have revealed the smallest LAT-based signaling units and nanostructure.

Indexed as

Adaptor Proteins, Signal TransducingMembrane ProteinsMultiprotein ComplexesAnimalsHumansNanostructuresProtein MultimerizationSignal TransductionAdaptor Proteins, Signal TransducingLAT protein, humanMembrane ProteinsMultiprotein Complexesadaptor proteincooperativityimmunologysignal transductionT-cell

Identifiers

PMID26354432
PMCPMC4646300
OpenAlexW1856616261

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.