Evidence map›Paper›PMID 8649391›Full record

ArticleMolecular and cellular biology1996

Tyrosine phosphorylation of Grb2-associated proteins correlates with phospholipase C gamma 1 activation in T cells.

D G Motto, M A Musci, S E Ross, G A Koretzky

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

11 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Altered peptide ligands act as partial agonists by inhibiting phospholipase C activity induced by myasthenogenic T cell epitopes.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  8. Article
  9. Article
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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.

D G MottoDepartment of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City 52242, USA.
M A Musci
S E Ross
G A Koretzky
University of Iowa · US

Funding

Multidisciplinary Lung Research Career Development ProgramT32HL007638 · NHLBI · UNIVERSITY OF IOWA · PI WELSH, MICHAEL J., ZABNER, JOSEPH · 1986 to 2020
$16.9M
NOVEL SUBSTRATES OF THE TCR KINASER01GM053256 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI KORETZKY, GARY A. · 1995 to 2005
$1.8M
CD45 REGULATION OF T-CELL RECEPTOR SIGNAL TRANSDUCTIONR01CA056050 · NCI · UNIVERSITY OF IOWA · PI KORETZKY, GARY A. · 1992 to 1994
–
NCI NIH HHS R01CA56050NHLBI NIH HHS HL07638NIGMS NIH HHS R01GM53256
6 · The paper itself

Abstract

Ligation of the T-cell antigen receptor (TCR) results in the rapid activation of several protein tyrosine kinases, with the subsequent phosphorylation of numerous cellular proteins. We investigated the requirement for tyrosine phosphorylation of proteins which bind the Grb2 SH2 domain in TCR-mediated signal transduction by transfecting the Jurkat T-cell line with a cDNA encoding a chimeric protein designed to dephosphorylate these molecules. Stimulation of the TCR on cells expressing this engineered enzyme fails to result in sustained tyrosine phosphorylation of a 36-kDa protein likely to be the recently cloned pp36/Lnk. Interestingly, TCR ligation of the transfected cells also fails to induce soluble inositol phosphate production and intracellular calcium mobilization, although receptor-mediated tyrosine phosphorylation of phospholipase C gamma 1 still occurs. TCR-mediated Ras and mitogen-activated protein kinase activation remain intact in cells expressing the engineered phosphatase. These data demonstrate that tyrosine phosphorylation of a protein(s) which binds the SH2 domain of Grb2 correlates with phospholipase C gamma 1 activation and suggest that such a phosphoprotein(s) plays a critical role in coupling the TCR with the phosphatidylinositol second-messenger pathway.

Indexed as

Adaptor Proteins, Signal TransducingBase SequenceCell LineDNA PrimersEnzyme ActivationGRB2 Adaptor ProteinHumansIntracellular Signaling Peptides and ProteinsIsoenzymesMolecular Sequence DataPhosphatidylinositolsPhospholipase C gammaPhosphoric Monoester HydrolasesPhosphorylationProtein BindingProteinsAdaptor Proteins, Signal TransducingDNA PrimersGRB2 Adaptor ProteinGRB2 protein, humanIntracellular Signaling Peptides and ProteinsIsoenzymesPhosphatidylinositolsPhospholipase C gammaPhosphoric Monoester HydrolasesProteinsras ProteinsReceptors, Antigen, T-CellRecombinant Fusion ProteinsSH2B3 protein, humanType C PhospholipasesTyrosine

Identifiers

PMID8649391
PMCPMC231274
OpenAlexW2124720131

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.