Evidence map›Paper›PMID 27711255›Full record

ArticlePloS one2016

Scaffold Role of DUSP22 in ASK1-MKK7-JNK Signaling Pathway.

Anna Ju, Young-Chang Cho, Ba Reum Kim, Sung Goo Park, Jeong-Hoon Kim, Kwonseop Kim, Jaehwi Lee, Byoung Chul Park, Sayeon Cho

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Frontiers in medicine · 2026
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  10. Review
  11. Clinical value of serum JKAP in acute ischemic stroke patients.Journal of clinical laboratory analysis · 2022
    Article
  12. Scaffolding of Mitogen-Activated Protein Kinase Signaling by β-Arrestins.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. RecurrentBlood · 2019
    Article
  18. Dual-Specificity Phosphatases in Immunity and Infection: An Update.International journal of molecular sciences · 2019
    Review
  19. Article
  20. Article
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

9 authors at 3 institutions in 1 country.

Anna JuCollege of Pharmacy, Chung-Ang University, Seoul, 06974, Republic of Korea.
Young-Chang ChoCollege of Pharmacy, Chung-Ang University, Seoul, 06974, Republic of Korea.
Ba Reum KimCollege of Pharmacy, Chung-Ang University, Seoul, 06974, Republic of Korea.
Sung Goo ParkDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 34141, Republic of Korea.
Jeong-Hoon KimPersonalized Genomic Medicine Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 34141, Republic of Korea.
Kwonseop KimCollege of Pharmacy and Research Institute for Drug Development, Chonnam National University, Gwangju, 61186, Republic of Korea.
Jaehwi LeeCollege of Pharmacy, Chung-Ang University, Seoul, 06974, Republic of Korea.
Byoung Chul ParkDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 34141, Republic of Korea.
Sayeon ChoCollege of Pharmacy, Chung-Ang University, Seoul, 06974, Republic of Korea.
Chung-Ang University · KRKorea Research Institute of Bioscience and Biotechnology · KRChonnam National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitogen-activated protein kinases (MAPKs) are involved in a variety of intracellular events such as gene expression, cell proliferation, and programmed cell death. MAPKs are activated by dual phosphorylation on threonine and tyrosine residues through sequential activation of protein kinases. Recent studies have shown that the protein kinases involved in MAPK signal transductions might be organized into signaling complexes by scaffold proteins. These scaffold proteins are essential regulators that function by assembling the relevant molecular components in mammalian cells. In this study, we report that dual-specificity phosphatase 22 (DUSP22), a member of the protein tyrosine phosphatase family, acts as a distinct scaffold protein in c-Jun N-terminal kinase (JNK) signaling. DUSP22 increased the phosphorylation in the activation loop of JNK regardless of its phosphatase activity but had no effect on phosphorylation levels of ERK and p38 in mammalian cells. Furthermore, DUSP22 selectively associated with apoptosis signal-regulating kinase 1 (ASK1), MAPK kinase 7 (MKK7), and JNK1/2. Both JNK phosphorylation and JNK-mediated apoptosis increased in a concentration-dependent manner regardless of DUSP22 phosphatase activity at low DUSP22 concentrations, but then decreased at higher DUSP22 concentrations, which is the prominent feature of a scaffold protein. Thus, our data suggest that DUSP22 regulates cell death by acting as a scaffold protein for the ASK1-MKK7-JNK signal transduction pathway independently of its phosphatase activity.

Indexed as

ApoptosisCaspase 3Cell SurvivalDual-Specificity PhosphatasesHCT116 CellsHEK293 CellsHumansHydrogen PeroxideImmunoprecipitationJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase 7MAP Kinase Kinase Kinase 5MAP Kinase Signaling SystemMitogen-Activated Protein Kinase PhosphatasesMutagenesis, Site-DirectedPhosphorylationCaspase 3Dual-Specificity PhosphatasesDUSP22 protein, humanHydrogen PeroxideJNK Mitogen-Activated Protein KinasesMAP2K7 protein, humanMAP3K5 protein, humanMAP Kinase Kinase 7MAP Kinase Kinase Kinase 5Mitogen-Activated Protein Kinase PhosphatasesPoly(ADP-ribose) Polymerases

Identifiers

PMID27711255
PMCPMC5053508
OpenAlexW2528545264

What OpenQuestion holds

Textmetadata
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.