Evidence map›Paper›PMID 27869819›Full record

ArticleNature immunology2017

A cycle of Zap70 kinase activation and release from the TCR amplifies and disperses antigenic stimuli.

Zachary B Katz, Lucie Novotná, Amy Blount, Björn F Lillemeier

Open access · greenAbstract read
In one paragraph

Article in Nature immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

53 citing papers in PubMed, 78 citations in OpenAlex.

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  15. Dephosphorylation accelerates the dissociation of ZAP70 from the T cell receptor.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

4 authors at 1 institution in 1 country.

Zachary B KatzNomis Center for Immunobiology and Microbial Pathogenesis &Waitt Advanced Biophotonics Center, Salk Institute for Biological Studies, La Jolla, California, USA.
Lucie NovotnáNomis Center for Immunobiology and Microbial Pathogenesis &Waitt Advanced Biophotonics Center, Salk Institute for Biological Studies, La Jolla, California, USA.
Amy BlountNomis Center for Immunobiology and Microbial Pathogenesis &Waitt Advanced Biophotonics Center, Salk Institute for Biological Studies, La Jolla, California, USA.
Björn F LillemeierNomis Center for Immunobiology and Microbial Pathogenesis &Waitt Advanced Biophotonics Center, Salk Institute for Biological Studies, La Jolla, California, USA.
Salk Institute for Biological Studies · US

Funding

Viral Vector Core (VVC)P30CA014195 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI Ye Zheng · 1985 to 2026
$82.8M
Salk Institute Cancer Training GrantT32CA009370 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI Diana Clare Hargreaves, Jan Karlseder · 1986 to 2026
$8.6M
Decipher membrane patterns in situ with super-resolution and dynamic microscopyDP2GM105455 · NIGMS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI LILLEMEIER, BJOERN F · 2012 to 2012
$2.9M
NCI NIH HHS P30 CA014195NCI NIH HHS T32 CA009370NIGMS NIH HHS DP2 GM105455
6 · The paper itself

Abstract

Cell-surface-receptor pathways amplify weak, rare and local stimuli to induce cellular responses. This task is accomplished despite signaling components that segregate into nanometer-scale membrane domains. Here we describe a 'catch-and-release' mechanism that amplified and dispersed stimuli by releasing activated kinases from receptors lacking intrinsic catalytic activity. Specifically, we discovered a cycle of recruitment, activation and release for Zap70 kinases at phosphorylated T cell antigen receptors (TCRs). This turned the TCR into a 'catalytic unit' that amplified antigenic stimuli. Zap70 released from the TCR remained at the membrane, translocated, and phosphorylated spatially distinct substrates. The mechanisms described here are based on widely used protein domains and post-translational modifications; therefore, many membrane-associated pathways might employ similar mechanisms for signal amplification and dispersion.

Indexed as

Activity CyclesAdaptor Proteins, Signal TransducingAnimalsAntigensHEK293 CellsHumansJurkat CellsLymphocyte ActivationMembrane ProteinsMiceMice, TransgenicPhosphoproteinsReceptor Cross-TalkReceptors, Antigen, T-CellSignal TransductionT-LymphocytesAdaptor Proteins, Signal TransducingAntigensLat protein, mouseMembrane ProteinsPhosphoproteinsReceptors, Antigen, T-CellZAP-70 Protein-Tyrosine Kinase

Identifiers

PMID27869819
PMCPMC5490839
OpenAlexW2550624787

What OpenQuestion holds

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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.