Evidence map›Paper›PMID 16467851›Full record

ArticleThe EMBO journal2006

Recruitment and activation of PLCgamma1 in T cells: a new insight into old domains.

Alex Braiman, Mira Barda-Saad, Connie L Sommers, Lawrence E Samelson

Abstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
–field-weighted citation impact
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

76 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Optogenetic control of PLC-γ1 activity polarizes cell motility.bioRxiv : the preprint server for biology · 2025
    Article
  5. [Latest Findings on the Role of Liquid-Liquid Phase Separation in the Regulation of Immune Cell Activation and Key Signaling].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2024
    Review
  6. Article
  7. Article
  8. Nerve Growth Factor and Autoimmune Diseases.Current issues in molecular biology · 2023
    Review
  9. 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
  10. Disrupted CaCellular & molecular immunology · 2023
    Article
  11. Pre-organized landscape of T cell surface.Frontiers in immunology · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Cbl-b Is Upregulated and Plays a Negative Role in Activated Human NK Cells.Journal of immunology (Baltimore, Md. : 1950) · 2021
    Article
  16. Review
  17. Wiskott-Aldrich Syndrome Protein: Roles in Signal Transduction in T Cells.Frontiers in cell and developmental biology · 2021
    Review
  18. Article
  19. Agent-Based Modeling of T Cell Receptor Cooperativity.International journal of molecular sciences · 2020
    Article
  20. Phospholipase C.Advances in experimental medicine and biology · 2020
    Review

16 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

4 authors.

Alex BraimanLaboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892-4254, USA.
Mira Barda-Saad
Connie L Sommers
Lawrence E Samelson

Funding

Biochemical Basis of T Cell ActivationZIABC010304 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SAMELSON, LAWRENCE · 2009 to 2025
$36.3M
BIOCHEMICAL BASIS OF T CELL ACTIVATIONZ01BC010304 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SAMELSON, LAWRENCE E · 1999 to 2008
$2.6M
Intramural NIH HHS
6 · The paper itself

Abstract

Engagement of the T-cell antigen receptor leads to recruitment of phospholipase Cgamma1 (PLCgamma1) to the LAT-nucleated signaling complex and to PLCgamma1 activation in a tyrosine phosphorylation-dependent manner. The mechanism of PLCgamma1 recruitment and the role of PLCgamma1 Src homology (SH) domains in this process remain incompletely understood. Using a combination of biochemical methods and real-time fluorescent imaging, we show here that the N-terminal SH2 domain of PLCgamma1 is necessary but not sufficient for its recruitment. Either the SH3 or C-terminal SH2 domain of PLCgamma1, with the participation of Vav1, c-Cbl and Slp76, are required to stabilize PLCgamma1 recruitment. All three PLCgamma1 SH domains are required for phosphorylation of PLCgamma1 Y783, which is critical for enzyme activation. These novel findings entailed revision of the currently accepted model of PLCgamma1 recruitment and activation in T lymphocytes.

Indexed as

Adaptor Proteins, Signal TransducingEnzyme ActivationHumansJurkat CellsLymphocyte ActivationMembrane ProteinsMicroscopy, FluorescencePhospholipase C gammaPhosphoproteinsPhosphorylationProtein Processing, Post-TranslationalProto-Oncogene Proteins c-cblProto-Oncogene Proteins c-vavReceptors, Antigen, T-CellSignal Transductionsrc Homology DomainsAdaptor Proteins, Signal TransducingCBL protein, humanLAT protein, humanMembrane ProteinsPhospholipase C gammaPhosphoproteinsProto-Oncogene Proteins c-cblProto-Oncogene Proteins c-vavReceptors, Antigen, T-CellVAV1 protein, human

Identifiers

PMID16467851
PMCPMC1383559

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.