Evidence map›Paper›PMID 17178161›Full record

ArticleMolecular immunology2007

Gelsolin overexpression alters actin dynamics and tyrosine phosphorylation of lipid raft-associated proteins in Jurkat T cells.

S Celeste Morley, Janice Sung, Guang-Ping Sun, Maria Paola Martelli, Stephen C Bunnell, Barbara E Bierer

Open access · greenAbstract read
In one paragraph

Article in Molecular immunology, 2007. 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
0.4field-weighted citation impact, top 37% 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, 19 citations in OpenAlex.

  1. Review
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  4. On the existence of endocytosis driven by membrane phase separations.Biochimica et biophysica acta. Biomembranes · 2020
    Review
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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

6 authors at 2 institutions in 1 country.

S Celeste MorleyLaboratory of Lymphocyte Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA. morley_c@kids.wustl.edu
Janice Sung
Guang-Ping Sun
Maria Paola Martelli
Stephen C Bunnell
Barbara E Bierer
National Institutes of Health · USNational Heart Lung and Blood Institute · US

Funding

PH D PROGRM IN IMMUNOLOGYT32CA009141 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI DORF, MARTIN E · 1985 to 1999
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Intramural NIH HHSNCI NIH HHS T32 CA009141NCI NIH HHS T32 CA09141
6 · The paper itself

Abstract

Upon T cell receptor engagement, both the actin cytoskeleton and substrates of tyrosine phosphorylation are remodeled to create a signaling complex at the interface of the antigen-presenting cell and responding T cell. While T cell signaling has been shown to regulate actin reorganization, the mechanisms by which changes in actin dynamics affect early T cell signaling have not been fully explored. Using gelsolin, an actin-binding protein with capping and severing activities, and latrunculin, an actin-depolymerizing agent, we have further investigated the interplay between actin dynamics and the regulation of T cell signaling. Overexpression of gelsolin altered actin dynamics in Jurkat T cells, and alteration of actin dynamics correlated with dysregulation of tyrosine phosphorylation of raft-associated substrates. This perturbation of tyrosine phosphorylation was correlated with inhibition of activation-dependent signaling pathways regulating Erk-1/2 phosphorylation, NF-AT transcriptional activation and IL-2 production. Modification of actin by the depolymerizing agent latrunculin also altered the tyrosine phosphorylation patterns of proteins associated with lipid rafts, and pre-treatment with latrunculin inhibited anti-CD3 mAb-mediated NF-AT activation. Thus, our data indicate that actin cytoskeletal dynamics modulate the tyrosine phosphorylation of raft-associated proteins and subsequent downstream signal transduction.

Indexed as

Gene ExpressionActinsAntibodies, MonoclonalBridged Bicyclo Compounds, HeterocyclicCD3 ComplexCytoskeletonDetergentsGelsolinHumansInterleukin-2Jurkat CellsMembrane MicrodomainsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Neoplasm ProteinsNFATC Transcription FactorsActinsAntibodies, MonoclonalBridged Bicyclo Compounds, HeterocyclicCD3 ComplexDetergentsGelsolinInterleukin-2latrunculin BMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Neoplasm ProteinsNFATC Transcription FactorsPhosphotyrosineThiazolidines

Identifiers

PMID17178161
PMCPMC1945820
OpenAlexW2049797247

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.