Evidence map›Paper›PMID 22499768›Full record

ArticleMolecular & cellular proteomics : MCP2012

Quantitative phosphoproteomic analysis reveals a role for serine and threonine kinases in the cytoskeletal reorganization in early T cell receptor activation in human primary T cells.

Patricia Ruperez, Ana Gago-Martinez, A L Burlingame, Juan A Oses-Prieto

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 43 citations in OpenAlex.

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  17. Protein networks and activation of lymphocytes.Current opinion in immunology · 2015
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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 2 institutions in 2 countries.

Patricia RuperezDepartment of Pharmaceutical Chemistry, Mass Spectrometry Facility, School of Pharmacy, University of California San Francisco, San Francisco, California 94158, USA.
Ana Gago-Martinez
A L Burlingame
Juan A Oses-Prieto
Universidade de Vigo · ESUniversity of California, San Francisco · US

Funding

YEAST THREONINE &SERINE KINASESP41RR001614 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ORTIZ DE MONTELLANO, PAUL R · 1985 to 2011
$24.1M
Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
PURCHASE OF Q TOF MASS SPECTROMETERS10RR012961 · NCRR · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI JAMES, THOMAS L · 1998 to 1998
–
NCRR NIH HHS P41 RR001614NCRR NIH HHS P41RR001614NCRR NIH HHS RR012961NIGMS NIH HHS P41 GM103481
6 · The paper itself

Abstract

Protein phosphorylation-dephosphorylation events play a primary role in regulation of almost all aspects of cell function including signal transduction, cell cycle, or apoptosis. Thus far, T cell phosphoproteomics have focused on analysis of phosphotyrosine residues, and little is known about the role of serine/threonine phosphorylation in early activation of the T cell receptor (TCR). Therefore, we performed a quantitative mass spectrometry-based analysis of the global phosphoproteome of human primary T cells in response to 5 min of TCR activation with anti-CD3 antibody. Combining immunoprecipitation with an antiphosphotyrosine antibody, titanium dioxide phosphopeptide enrichment, isobaric tag for the relative and absolute quantitation methodology, and strong cation exchange separation, we were able to identify 2814 phosphopeptides. These unique sites were employed to investigate the site-specific phosphorylation dynamics. Five hundred and seventeen phosphorylation sites showed TCR-responsive changes. We found that upon 5 min of stimulation of the TCR, specific serine and threonine kinase motifs are overrepresented in the set of responsive phosphorylation sites. These phosphorylation events targeted proteins with many different activities and are present in different subcellular locations. Many of these proteins are involved in intracellular signaling cascades related mainly to cytoskeletal reorganization and regulation of small GTPase-mediated signal transduction, probably involved in the formation of the immune synapse.

Indexed as

Amino Acid SequenceAntilymphocyte SerumCD3 ComplexCells, CulturedChromatography, AffinityCluster AnalysisConsensus SequenceCytoskeletonHumansLymphocyte ActivationPeptide FragmentsPhosphoproteinsPrimary Cell CultureProtein Interaction MapsProtein Serine-Threonine KinasesProteomeAntilymphocyte SerumCD3 ComplexPeptide FragmentsPhosphoproteinsProtein Serine-Threonine KinasesProteomeReceptors, Antigen, T-Cell

Identifiers

PMID22499768
PMCPMC3418841
OpenAlexW2165640627

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.