Evidence map›Paper›PMID 9813084›Full record

ArticleThe Journal of cell biology1998

ZAP-70 association with T cell receptor zeta (TCRzeta): fluorescence imaging of dynamic changes upon cellular stimulation.

J Sloan-Lancaster, J Presley, J Ellenberg, T Yamazaki, J Lippincott-Schwartz, L E Samelson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

26 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. 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
    Article
  7. A cell topography-based mechanism for ligand discrimination by the T cell receptor.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. ZAP-70: an essential kinase in T-cell signaling.Cold Spring Harbor perspectives in biology · 2010
    Review
  17. Article
  18. Article
  19. Article
  20. Feedback control of T-cell receptor activation.Proceedings. Biological sciences · 2004
    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.

J Sloan-LancasterThe Section on Lymphocyte Signaling, Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA.
J Presley
J Ellenberg
T Yamazaki
J Lippincott-Schwartz
L E Samelson
National Institutes of Health · US

Funding

Texas Tech Center for Translational Research and Rural Health - Research Capacity CoreU54MD020892 · NIMHD · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI Lance R. McMahon, Naima Moustaid-Moussa · 2026 to 2026
$10.0M
NIMHD NIH HHS U54 MD020892
6 · The paper itself

Abstract

The nonreceptor protein tyrosine kinase ZAP-70 is a critical enzyme required for successful T lymphocyte activation. After antigenic stimulation, ZAP-70 rapidly associates with T cell receptor (TCR) subunits. The kinetics of its translocation to the cell surface, the properties of its specific interaction with the TCRzeta chain expressed as a chimeric protein (TTzeta and Tzetazeta), and its mobility in different intracellular compartments were studied in individual live HeLa cells, using ZAP-70 and Tzetazeta fused to green fluorescent protein (ZAP-70 GFP and Tzetazeta-GFP, respectively). Time-lapse imaging using confocal microscopy indicated that the activation-induced redistribution of ZAP-70 to the plasma membrane, after a delayed onset, is of long duration. The presence of the TCRzeta chain is critical for the redistribution, which is enhanced when an active form of the protein tyrosine kinase Lck is coexpressed. Binding specificity to TTzeta was indicated using mutant ZAP-70 GFPs and a truncated zeta chimera. Photobleaching techniques revealed that ZAP-70 GFP has decreased mobility at the plasma membrane, in contrast to its rapid mobility in the cytosol and nucleus. Tzetazeta- GFP is relatively immobile, while peripherally located ZAP-70 in stimulated cells is less mobile than cytosolic ZAP-70 in unstimulated cells, a phenotype confirmed by determining the respective diffusion constants. Examination of the specific molecular association of signaling proteins using these approaches has provided new insights into the TCRzeta-ZAP-70 interaction and will be a powerful tool for continuing studies of lymphocyte activation.

Indexed as

ActinsCell MembraneCytoskeletonCytosolGene ExpressionGreen Fluorescent ProteinsHeLa CellsHumansImage Processing, Computer-AssistedIndicators and ReagentsLuminescent ProteinsLymphocyte Specific Protein Tyrosine Kinase p56(lck)Membrane ProteinsMicrotubulesProtein-Tyrosine KinasesReceptors, Antigen, T-CellActinsantigen T cell receptor, zeta chainGreen Fluorescent ProteinsIndicators and ReagentsLuminescent ProteinsLymphocyte Specific Protein Tyrosine Kinase p56(lck)Membrane ProteinspervanadateProtein-Tyrosine KinasesReceptors, Antigen, T-CellRecombinant Fusion ProteinsVanadatesZAP70 protein, humanZAP-70 Protein-Tyrosine Kinase

Identifiers

PMID9813084
PMCPMC2148150
OpenAlexW2128967976

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.