Evidence map›Paper›PMID 25993510›Full record

ArticlePloS one2015

Reciprocal regulation of C-Maf tyrosine phosphorylation by Tec and Ptpn22.

Chih-Chun Liu, Chen-Yen Lai, Wei-Feng Yen, Yu-Hsien Lin, Hui-Hsin Chang, Tzong-Shyuan Tai, Yu-Jung Lu, Hsiao-Wei Tsao, I-Cheng Ho, Shi-Chuen Miaw

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

7 citing papers in PubMed, 8 citations in OpenAlex.

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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

10 authors at 3 institutions in 2 countries.

Chih-Chun LiuGraduate Institute of Immunology, National Taiwan University College of Medicine, Taipei, Taiwan.
Chen-Yen LaiGraduate Institute of Immunology, National Taiwan University College of Medicine, Taipei, Taiwan.
Wei-Feng YenGraduate Institute of Immunology, National Taiwan University College of Medicine, Taipei, Taiwan.
Yu-Hsien LinGraduate Institute of Immunology, National Taiwan University College of Medicine, Taipei, Taiwan.
Hui-Hsin ChangDivision of Rheumatology, Immunology and Allergy, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, United States of America.
Tzong-Shyuan TaiDivision of Rheumatology, Immunology and Allergy, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, United States of America.
Yu-Jung LuGraduate Institute of Immunology, National Taiwan University College of Medicine, Taipei, Taiwan.
Hsiao-Wei TsaoGraduate Institute of Immunology, National Taiwan University College of Medicine, Taipei, Taiwan.
I-Cheng HoDivision of Rheumatology, Immunology and Allergy, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, United States of America.
Shi-Chuen MiawGraduate Institute of Immunology, National Taiwan University College of Medicine, Taipei, Taiwan.
National Taiwan University · TWBrigham and Women's Hospital · USHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

C-Maf plays an important role in regulating cytokine production in TH cells. Its transactivation of IL-4 is optimized by phosphorylation at Tyr21, Tyr92, and Tyr131. However, the molecular mechanism regulating its tyrosine phosphorylation remains unknown. In this study, we demonstrate that Tec kinase family member Tec, but not Rlk or Itk, is a tyrosine kinase of c-Maf and that Tec enhances c-Maf-dependent IL-4 promoter activity. This effect of Tec is counteracted by Ptpn22, which physically interacts with and facilitates tyrosine dephosphorylation of c-Maf thereby attenuating its transcriptional activity. We further show that phosphorylation of Tyr21/92/131 of c-Maf is also critical for its recruitment to the IL-21 promoter and optimal production of this cytokine by TH17 cells. Thus, manipulating tyrosine phosphorylation of c-Maf through its kinases and phosphatases can have significant impact on TH cell-mediated immune responses.

Indexed as

AnimalsCell NucleusHEK293 CellsHumansInterleukin-21Interleukin-4InterleukinsMice, Inbred C57BLMice, KnockoutPhosphorylationPhosphotyrosinePromoter Regions, GeneticProtein BindingProtein-Tyrosine KinasesProtein Tyrosine Phosphatase, Non-Receptor Type 22Proto-Oncogene Proteins c-mafInterleukin-21Interleukin-4InterleukinsPhosphotyrosineProtein-Tyrosine KinasesProtein Tyrosine Phosphatase, Non-Receptor Type 22Proto-Oncogene Proteins c-mafPtpn22 protein, mouseTec protein-tyrosine kinase

Identifiers

PMID25993510
PMCPMC4439128
OpenAlexW1832571610

What OpenQuestion holds

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LicenceCC BY
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.