Evidence map›Paper›PMID 40935154›Full record

ArticleMolecular & cellular proteomics : MCP2025

Mycobacterial Tyrosine Phosphatase PtpB Affects Host Cytokine Expression by Dephosphorylating ERK1/2 and STAT3.

Tianxian Liu, Yameng Fan, Yijia Chen, Shuyu Xie, Jun-Yu Xu, Minjia Tan, Bang-Ce Ye

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. Secreted proteins ofFrontiers in tuberculosis · 2026
    Review
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

7 authors.

Tianxian LiuLaboratory of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China; State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Yameng FanState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Yijia ChenLaboratory of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.
Shuyu XieState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Jun-Yu XuState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China; Zhongshan Institute for Drug Discovery, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Zhongshan, China. Electronic address: jyxu@simm.ac.cn.
Minjia TanState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China; Zhongshan Institute for Drug Discovery, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Zhongshan, China. Electronic address: mjtan@simm.ac.cn.
Bang-Ce YeLaboratory of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China. Electronic address: bcye@ecust.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mycobacterium tuberculosis (Mtb) tyrosine phosphatases PtpA and PtpB have been widely reported to affect host immunity response and bacterial intercellular survival. However, a comprehensive investigation into the impact of PtpA and PtpB on host phosphorylation, specifically in their roles as tyrosine phosphatases, has not yet been reported. In this study, we first conducted the potential dephosphorylation substrates map of PtpA and PtpB within the host. Our findings demonstrated that PtpB significantly decreased the phosphorylation levels of ERK1/2 and STAT3. Subsequent analysis indicated that PtpB modulated the production of cytokine TNF and IL-1β by dephosphorylating ERK1/2 and preventing its nuclear translocation. PtpB also reduced IL-6 and IL-1β expression by dephosphorylating STAT3. The in vivo experiment demonstrated increased bacterial survival and reduced cytokine expression in the PtpB-overexpression strain. Consequently, our findings demonstrate that Mtb tyrosine phosphatases PtpA and PtpB play critical roles in the global tyrosine phosphorylation landscape within the host. Specifically, PtpB modulates cytokine expression through the dephosphorylation of ERK1/2 and STAT3.

Indexed as

Bacterial ProteinsCytokinesMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mycobacterium tuberculosisProtein Tyrosine PhosphatasesSTAT3 Transcription FactorAnimalsHost-Pathogen InteractionsHumansInterleukin-1betaMicePhosphorylationBacterial ProteinsCytokinesInterleukin-1betaMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3MptpA protein, Mycobacterium tuberculosisProtein Tyrosine PhosphatasesSTAT3 Transcription FactorERK1/2immune responsemycobacteriatyrosine phosphatases PtpBtyrosine phosphoproteomic

Identifiers

PMID40935154
PMCPMC12546780

What OpenQuestion holds

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Registered trials

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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.