ArticleProtein science : a publication of the Protein Society2011
GST pi modulates JNK activity through a direct interaction with JNK substrate, ATF2.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 46 citations in OpenAlex.
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- Mechanism of influence of calcified nanoparticles in the development of calcified diseases (Review).Biomedical reports · 2025Review
- Underlying mechanisms and treatment of acetaminophen‑induced liver injury (Review).Molecular medicine reports · 2025Review
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- Resveratrol and N-acetylcystein reduce hepatic steatosis but enhance initiation and progression of hepatocellular carcinoma by inhibiting GST-pi-MAPK axis in mice.Frontiers in pharmacology · 2025Article
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- Tat-GSTpi Inhibits Dopaminergic Cells against MPPBiomedicines · 2023Article
- The good Samaritan glutathione-S-transferase P1: An evolving relationship in nitric oxide metabolism mediated by the direct interactions between multiple effector molecules.Redox biology · 2023Review
- Glutathione S-Transferase P1 Genetic Variant's Influence on the HbA1c Level in Type Two Diabetic Patients.International journal of environmental research and public health · 2023Article
- Antioxidant Genetic Profile Modifies Probability of Developing Neurological Sequelae in Long-COVID.Antioxidants (Basel, Switzerland) · 2022Article
- Glutathione S-transferase Pi (Gstp) proteins regulate neuritogenesis in the developing cerebral cortex.Human molecular genetics · 2021Article
- Protein Lipoxidation: Basic Concepts and Emerging Roles.Antioxidants (Basel, Switzerland) · 2021Review
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- The Association of Polymorphisms inOxidative medicine and cellular longevity · 2021Article
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- Glutathione Transferase P1 Polymorphism Might Be a Risk Determinant in Heart Failure.Disease markers · 2019Article
- Glutathione Transferases: Potential Targets to Overcome Chemoresistance in Solid Tumors.International journal of molecular sciences · 2018Review
- Glutathione S-transferase P deficiency induces glucose intolerance via JNK-dependent enhancement of hepatic gluconeogenesis.American journal of physiology. Endocrinology and metabolism · 2018Article
- Role of microRNA-21 in uveal melanoma cell invasion and metastasis by regulating p53 and its downstream protein.International journal of ophthalmology · 2018Article
- GSTP1 exon 5 rs200139798 polymorphism and clinicopathological characteristics of gastric cancer in Chinese patients.International journal of clinical and experimental pathology · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Human GSTpi, an important detoxification enzyme, has been shown to modulate the activity of JNKs by inhibiting apoptosis and by causing cell proliferation and tumor growth. In this work, we describe a detailed analysis of the interaction in vitro between GSTpi and JNK isoforms (both in their inactive and active, phosphorylated forms). The ability of active JNK1 or JNK2 to phosphorylate their substrate, ATF2, is inhibited by two naturally occurring GSTpi haplotypes (Ile105/Ala114, WT or haplotype A, and Val105/Val114, haplotype C). Haplotype C of GSTpi is a more potent inhibitor of JNK activity than haplotype A, yielding 75-80% and 25-45% inhibition, respectively. We show that GSTpi is not a substrate of JNK, as was earlier suggested by others. Through binding studies, we demonstrate that the interaction between GSTpi and phosphorylated, active JNKs is isoform specific, with JNK1 being the preferred isoform. In contrast, GSTpi does not interact with unphosphorylated, inactive JNKs unless a JNK substrate, ATF2, is present. We also demonstrate, for the first time, a direct interaction: between GSTpi and ATF2. GSTpi binds with similar affinity to active JNK + ATF2 and to ATF2 alone. Direct binding experiments between ATF2 and GSTpi, either alone or in the presence of glutathione analogs or phosphorylated ATF2, indicate that the xenobiotic portion of the GSTpi active site and the JNK binding domain of ATF2 are involved in this interaction. Competition between GSTpi and active JNK for the substrate ATF2 may be responsible for the inhibition of JNK catalysis by GSTpi.
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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.