Evidence map›Paper›PMID 11564877›Full record

ArticleMolecular and cellular biology2001

Membrane raft-dependent regulation of phospholipase Cgamma-1 activation in T lymphocytes.

M C Verí, K E DeBell, M C Seminario, A DiBaldassarre, I Reischl, R Rawat, L Graham, C Noviello, B L Rellahan, S Miscia and 2 more

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

21 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
  3. Noncatalytic Bruton's tyrosine kinase activates PLCγThe Journal of biological chemistry · 2020
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  9. Review
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  12. Article
  13. A critical role for the E3-ligase activity of c-Cbl in VEGFR-2-mediated PLCgamma1 activation and angiogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  14. Article
  15. Lipid rafts and regulation of the cytoskeleton during T cell activation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2005
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

12 authors at 3 institutions in 2 countries.

M C VeríLaboratory of Immunobiology, Division of Monoclonal Antibodies, Center for Biologics Evaluation & Research, National Institute o f Health, Bethesda, Maryland 20892, USA.
K E DeBell
M C Seminario
A DiBaldassarre
I Reischl
R Rawat
L Graham
C Noviello
B L Rellahan
S Miscia
R L Wange
E Bonvini
Center for Biologics Evaluation and Research · USNational Institutes of Health · USUniversity of Chieti-Pescara · IT

Funding

REGULATION OF T CELL ACTIVATIONZ01AG000509 · NIA · AGING · PI WANGE, RONALD L. · 1997 to 2004
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6 · The paper itself

Abstract

Numerous signaling molecules associate with lipid rafts, either constitutively or after engagement of surface receptors. One such molecule, phospholipase Cgamma-1 (PLCgamma1), translocates from the cytosol to lipid rafts during T-cell receptor (TCR) signaling. To investigate the role played by lipid rafts in the activation of this molecule in T cells, an influenza virus hemagglutinin A (HA)-tagged PLCgamma1 was ectopically expressed in Jurkat T cells and targeted to these microdomains by the addition of a dual-acylation signal. Raft-targeted PLCgamma1 was constitutively tyrosine phosphorylated and induced constitutive NF-AT-dependent transcription and interleukin-2 secretion in Jurkat cells. Tyrosine phosphorylation of raft-targeted PLCgamma1 did not require Zap-70 or the interaction with the adapters Lat and Slp-76, molecules that are necessary for TCR signaling. In contrast, the Src family kinase Lck was required. Coexpression in HEK 293T cells of PLCgamma1-HA with Lck or the Tec family kinase Rlk resulted in preferential phosphorylation of raft-targeted PLCgamma1 over wild-type PLCgamma1. These data show that localization of PLCgamma1 in lipid rafts is sufficient for its activation and demonstrate a role for lipid rafts as microdomains that dynamically segregate and integrate PLCgamma1 with other signaling components.

Indexed as

Adaptor Proteins, Signal TransducingMembrane ProteinsNuclear ProteinsAcylationCalciumCarrier ProteinsCell LineDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelEnzyme ActivationEnzyme-Linked Immunosorbent AssayGene Expression Regulation, EnzymologicHumansImmunoblottingInterleukin-2IsoenzymesAdaptor Proteins, Signal TransducingCalciumCarrier ProteinsDNA-Binding ProteinsInterleukin-2IsoenzymesLAT protein, humanLuciferasesMembrane ProteinsNFATC Transcription FactorsNuclear ProteinsPhospholipase C gammaPhosphoproteinsProtein-Tyrosine KinasesSLP-76 signal Transducing adaptor proteinsTranscription FactorsType C PhospholipasesTyrosineZAP70 protein, humanZAP-70 Protein-Tyrosine Kinase

Identifiers

PMID11564877
PMCPMC99870
OpenAlexW2145385074

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.