Evidence map›Paper›PMID 20562827›Full record

ArticleThe EMBO journal2010

Cooperative interactions at the SLP-76 complex are critical for actin polymerization.

Mira Barda-Saad, Naoto Shirasu, Maor H Pauker, Nirit Hassan, Orly Perl, Andrea Balbo, Hiroshi Yamaguchi, Jon C D Houtman, Ettore Appella, Peter Schuck and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

73 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. 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
  8. Review
  9. T cell receptor (TCR) signaling in health and disease.Signal transduction and targeted therapy · 2021
    Review
  10. Article
  11. Nck adaptors at a glance.Journal of cell science · 2021
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Enhancing network activation in natural killer cells: predictions from in silico modeling.Integrative biology : quantitative biosciences from nano to macro · 2020
    Article
  17. Article
  18. Review
  19. Article
  20. Cooperative assembly of a four-molecule signaling complex formed upon T cell antigen receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article

13 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

11 authors at 5 institutions in 2 countries.

Mira Barda-SaadMina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan, Israel. bardasm@mail.biu.ac.il
Naoto Shirasu
Maor H Pauker
Nirit Hassan
Orly Perl
Andrea Balbo
Hiroshi Yamaguchi
Jon C D Houtman
Ettore Appella
Peter Schuck
Lawrence E Samelson
Bar-Ilan University · ILCenter for Cancer Research · USNational Institute of Biomedical Imaging and Bioengineering · USNational Institutes of Health · USUniversity of Iowa · US

Funding

Biochemical Basis of T Cell ActivationZIABC010304 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SAMELSON, LAWRENCE · 2009 to 2025
$36.3M
Biophysical Characterization Of MacromoleculesZICEB000008 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2010 to 2010
$427k
Intramural NIH HHS
6 · The paper itself

Abstract

T-cell antigen receptor (TCR) engagement induces formation of multi-protein signalling complexes essential for regulating T-cell functions. Generation of a complex of SLP-76, Nck and VAV1 is crucial for regulation of the actin machinery. We define the composition, stoichiometry and specificity of interactions in the SLP-76, Nck and VAV1 complex. Our data reveal that this complex can contain one SLP-76 molecule, two Nck and two VAV1 molecules. A direct interaction between Nck and VAV1 is mediated by binding between the C-terminal SH3 domain of Nck and the VAV1 N-terminal SH3 domain. Disruption of the VAV1:Nck interaction deleteriously affected actin polymerization. These novel findings shed new light on the mechanism of actin polymerization after T-cell activation.

Indexed as

ActinsAdaptor Proteins, Signal TransducingAnimalsHumansJurkat CellsLymphocyte ActivationOncogene ProteinsPhosphoproteinsProtein BindingProto-Oncogene Proteins c-vavReceptors, Antigen, T-CellRecombinant Fusion ProteinsSignal Transductionsrc Homology DomainsT-LymphocytesActinsAdaptor Proteins, Signal TransducingNck proteinOncogene ProteinsPhosphoproteinsProto-Oncogene Proteins c-vavReceptors, Antigen, T-CellRecombinant Fusion ProteinsSLP-76 signal Transducing adaptor proteinsVAV1 protein, human

Identifiers

PMID20562827
PMCPMC2910278
OpenAlexW2142077075

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.