Evidence map›Paper›PMID 19324872›Full record

ArticleThe Journal of biological chemistry2009

T cell receptor-mediated activation of p38{alpha} by mono-phosphorylation of the activation loop results in altered substrate specificity.

Paul R Mittelstadt, Hiroshi Yamaguchi, Ettore Appella, Jonathan D Ashwell

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

34 citing papers in PubMed, 49 citations in OpenAlex.

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  7. MK2 degradation as a sensor of signal intensity that controls stress-induced cell fate.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  16. Intensity and duration of TCR signaling is limited by p38 phosphorylation of ZAP-70Proceedings of the National Academy of Sciences of the United States of America · 2018
    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.

Paul R MittelstadtLaboratory of Immune Cell Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892, USA.
Hiroshi Yamaguchi
Ettore Appella
Jonathan D Ashwell
National Institutes of Health · US

Funding

Tumor Suppressor Protein, p53ZIABC005599 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI APPELLA, ETTORE · 2009 to 2025
$8.1M
T Cell Alternative p38 Activation PathwayZIABC010774 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI ASHWELL, JONATHAN · 2009 to 2019
$6.2M
TUMOR SUPPRESSOR PROTEIN, P53Z01BC005599 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI APPELLA, ETTORE · 1996 to 2008
$1.6M
T Cell Alternative p38 Activation PathwayZ01BC010774 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI ASHWELL, JONATHAN · 2007 to 2008
$1.3M
6 · The paper itself

Abstract

p38 MAPKs are typically activated by upstream MAPK kinases that phosphorylate a Thr-X-Tyr motif in the activation loop. An exception is the T cell antigen receptor signaling pathway, which bypasses the MAPK cascade and activates p38alpha and p38beta by phosphorylation of Tyr-323 and subsequent autophosphorylation of the activation loop. Here we show that, unlike the classic MAPK cascade, the alternative pathway results primarily in mono-phosphorylation of the activation loop residue Thr-180. Recombinant mono-phosphorylated and dual phosphorylated p38alpha differed widely with regard to activity and substrate preference. Altered substrate specificity was reproduced in T cells in which p38 was activated by the alternative or classical MAPK pathways. These findings suggest that T cells have evolved a mechanism to utilize p38 in a specialized manner independent of and distinct from the classical p38 MAPK signaling cascade.

Indexed as

Adenosine TriphosphateAnimalsEnzyme ActivationHumansKineticsMiceMice, Inbred C57BLp38 Mitogen-Activated Protein KinasesPhosphorylationReceptors, Antigen, T-CellRecombinant ProteinsSignal TransductionSubstrate SpecificityTetradecanoylphorbol AcetateThreonineT-LymphocytesAdenosine Triphosphatep38 Mitogen-Activated Protein KinasesReceptors, Antigen, T-CellRecombinant ProteinsTetradecanoylphorbol AcetateThreonineTyrosine

Identifiers

PMID19324872
PMCPMC2708844
OpenAlexW1978021679

What Socratic 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 Socratic graph.