Evidence map›Paper›PMID 25266776›Full record

ArticleMolecular & cellular proteomics : MCP2014

Quantitative phosphoproteomics of cytotoxic T cells to reveal protein kinase d 2 regulated networks.

María N Navarro, Juergen Goebel, Jens L Hukelmann, Doreen A Cantrell

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. A Rapid Translational Immune Response Program in CD8 Memory T Lymphocytes.Journal of immunology (Baltimore, Md. : 1950) · 2022
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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.

María N NavarroFrom the ‡Division of Cell Signalling and Immunology. College of Life Sciences University of Dundee, Dundee, Scotland, U.K.
Juergen GoebelFrom the ‡Division of Cell Signalling and Immunology. College of Life Sciences University of Dundee, Dundee, Scotland, U.K.
Jens L HukelmannFrom the ‡Division of Cell Signalling and Immunology. College of Life Sciences University of Dundee, Dundee, Scotland, U.K.
Doreen A CantrellFrom the ‡Division of Cell Signalling and Immunology. College of Life Sciences University of Dundee, Dundee, Scotland, U.K. d.a.cantrell@dundee.ac.uk.
University of Dundee · GB

Funding

Wellcome Trust 065975/Z/01/AWellcome Trust 097418Wellcome Trust 097418/Z/11Z
6 · The paper itself

Abstract

The focus of the present study was to characterize the phosphoproteome of cytotoxic T cells and to explore the role of the serine threonine kinase PKD2 (Protein Kinase D2) in the phosphorylation networks of this key lymphocyte population. We used Stable Isotope Labeling of Amino acids in Culture (SILAC) combined with phosphopeptide enrichment and quantitative mass-spectrometry to determine the impact of PKD2 loss on the cytotoxic T cells phosphoproteome. We identified 15,871 phosphorylations on 3505 proteins in cytotoxic T cells. 450 phosphosites on 281 proteins were down-regulated and 300 phosphosites on 196 proteins were up-regulated in PKD2 null cytotoxic T cells. These data give valuable new insights about the protein phosphorylation networks operational in effector T cells and reveal that PKD2 regulates directly and indirectly about 5% of the cytotoxic T-cell phosphoproteome. PKD2 candidate substrates identified in this study include proteins involved in two distinct biological functions: regulation of protein sorting and intracellular vesicle trafficking, and control of chromatin structure, transcription, and translation. In other cell types, PKD substrates include class II histone deacetylases such as HDAC7 and actin regulatory proteins such as Slingshot. The current data show these are not PKD substrates in primary T cells revealing that the functional role of PKD isoforms is different in different cell lineages.

Indexed as

Gene Regulatory NetworksAnimalsAntibodiesCarbon IsotopesCD3 ComplexGene Expression RegulationHistone DeacetylasesIsotope LabelingLymphocyte ActivationMiceMice, TransgenicNitrogen IsotopesOrgan SpecificityPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationAntibodiesCarbon IsotopesCD3 ComplexHdac7 protein, mouseHistone DeacetylasesNitrogen IsotopesPhosphoprotein PhosphatasesPhosphoproteinsProteomeTRPP Cation Channels

Identifiers

PMID25266776
PMCPMC4256504
OpenAlexW2158898632

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.