ArticleOncogene2002
Dual-specificity protein tyrosine phosphatase VHR down-regulates c-Jun N-terminal kinase (JNK).
Article in Oncogene, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 60 citations in OpenAlex.
- Review
- DUSP family phosphatases in cell signaling, inflammation, and chronic diseases.Journal of biomedical science · 2026Review
- Article
- Differential aortic aneurysm formation provoked by chemogenetic oxidative stress.The Journal of clinical investigation · 2025Article
- DUSP3 regulates phosphorylation-mediated degradation of occludin and is required for maintaining epithelial tight junction.Journal of biomedical science · 2022Article
- Regulation of signal transducer and activator of transcription 3 activation by dual-specificity phosphatase 3.BMB reports · 2020Article
- Allosteric Impact of the Variable Insert Loop inBiochemistry · 2020Article
- Phosphorylation Dynamics of JNK Signaling: Effects of Dual-Specificity Phosphatases (DUSPs) on the JNK Pathway.International journal of molecular sciences · 2019Review
- Dual-Specificity Phosphatases in Immunity and Infection: An Update.International journal of molecular sciences · 2019Review
- Deficiency in VHR/DUSP3, a suppressor of focal adhesion kinase, reveals its role in regulating cell adhesion and migration.Oncogene · 2017Article
- Dusp3 deletion in mice promotes experimental lung tumour metastasis in a macrophage dependent manner.PloS one · 2017Article
- Perspective: Tyrosine phosphatases as novel targets for antiplatelet therapy.Bioorganic & medicinal chemistry · 2015Review
- Cellular biochemistry methods for investigating protein tyrosine phosphatases.Antioxidants & redox signaling · 2014Review
- KDM2A promotes lung tumorigenesis by epigenetically enhancing ERK1/2 signaling.The Journal of clinical investigation · 2013Article
- Specificity profiling of protein phosphatases toward phosphoseryl and phosphothreonyl peptides.Journal of the American Chemical Society · 2013Article
- Specificity profiling of dual specificity phosphatase vaccinia VH1-related (VHR) reveals two distinct substrate binding modes.The Journal of biological chemistry · 2013Article
- Protein tyrosine phosphatases--from housekeeping enzymes to master regulators of signal transduction.The FEBS journal · 2013Review
- Small molecule tools for functional interrogation of protein tyrosine phosphatases.The FEBS journal · 2013Review
- DUSP13B/TMDP inhibits stress-activated MAPKs and suppresses AP-1-dependent gene expression.Molecular and cellular biochemistry · 2011Article
- Vaccinia H1-related phosphatase is a phosphatase of ErbB receptors and is down-regulated in non-small cell lung cancer.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The JNK group (for c-Jun N-terminal kinase) of mitogen-activated protein kinases (MAP kinases) is activated in cells in response to environmental stress and cytokines. Activation of JNK is the result of dual phosphorylation by specific upstream kinases which phosphorylate the TxY motif. Much less is known concerning the down-regulation by protein phosphatases. Here, we demonstrate that the tyrosine-specific and constitutively-expressed phosphatase VHR (for VH1-Related) down-regulates the JNK signaling pathway at the level of JNK dephosphorylation. VHR was shown to efficiently dephosphorylate JNK and to form a tight complex with activated JNK when the catalytically-inactive C124S VHR mutant was employed as an in vivo substrate trap. Utilizing an in vitro assay, the transcription factor c-Jun specifically inhibited the ability of VHR to dephosphorylate JNK, likely by sterically blocking access to the phosphorylation sites when JNK and c-Jun form a complex. c-Jun has no effect on the ability of VHR to inactivate the ERK MAP kinases or to hydrolyze artificial substrates. The c-Jun inhibition results are discussed in terms of the resistant-nature of JNK dephosphorylation in cellular extracts and in terms of a general model in which VHR may be a general MAP kinase phosphatase whose specificity and activity are dictated by the presence of MAP kinase-associated proteins that inhibit dephosphorylation.
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Registered trials
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.