ArticleHandbook of experimental pharmacology2014
Arrestin-dependent activation of JNK family kinases.
Article in Handbook of experimental pharmacology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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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.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- Mechanisms of Location Bias in G Protein-Coupled Receptors.Handbook of experimental pharmacology · 2026Review
- Arrestin-3-assisted activation of JNK3 mediates dopaminergic behavioral sensitization.Cell reports. Medicine · 2024Article
- Surveying nonvisual arrestins reveals allosteric interactions between functional sites.Proteins · 2023Article
- Short Arrestin-3-Derived Peptides Activate JNK3 in Cells.International journal of molecular sciences · 2022Article
- Colocalization and Interaction Study of Neuronal JNK3, JIP1, and β-Arrestin2 Together with PSD95.International journal of molecular sciences · 2022Article
- A non-GPCR-binding partner interacts with a novel surface on β-arrestin1 to mediate GPCR signaling.The Journal of biological chemistry · 2020Article
- JNK and cardiometabolic dysfunction.Bioscience reports · 2019Review
- Arrestin-3 scaffolding of the JNK3 cascade suggests a mechanism for signal amplification.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural basis of arrestin-3 activation and signaling.Nature communications · 2017Article
- G Protein-Coupled Receptor Signaling Through β-Arrestin-Dependent Mechanisms.Journal of cardiovascular pharmacology · 2017Review
- Functional competence of a partially engaged GPCR-β-arrestin complex.Nature communications · 2016Article
- Regulation of N-Formyl Peptide Receptor Signaling and Trafficking by Arrestin-Src Kinase Interaction.PloS one · 2016Article
- Multifaceted role of β-arrestins in inflammation and disease.Genes and immunity · 2015Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The activity of all mitogen-activated protein kinases (MAPKs) is stimulated via phosphorylation by upstream MAPK kinases (MAPKK), which are in their turn activated via phosphorylation by MAPKK kinases (MAPKKKs). The cells ensure the specificity of signaling in these cascades by employing a variety of scaffolding proteins that bind matching MAPKKKs, MAPKKs, and MAPKs. All four vertebrate arrestin subtypes bind JNK3, but only arrestin-3 serves as a scaffold, promoting JNK3 activation in intact cells. Arrestin-3-mediated JNK3 activation does not depend on arrestin-3 interaction with G protein-coupled receptors (GPCRs), as demonstrated by the ability of some arrestin mutants that cannot bind receptors to activate JNK3, whereas certain mutants with enhanced GPCR binding fail to promote JNK3 activation. Recent findings suggest that arrestin-3 directly binds both MAPKKs necessary for JNK activation and facilitates JNK3 phosphorylation at both Thr (by MKK4) and Tyr (by MKK7). JNK3 is expressed in a limited set of cell types, whereas JNK1 and JNK2 isoforms are as ubiquitous as arrestin-3. Recent study showed that arrestin-3 facilitates the activation of JNK1 and JNK2, scaffolding MKK4/7-JNK1/2/3 signaling complexes. In all cases, arrestin-3 acts by bringing the kinases together: JNK phosphorylation shows biphasic dependence on arrestin-3, being enhanced at lower and suppressed at supraoptimal concentrations. Thus, arrestin-3 regulates the activity of multiple JNK isoforms, suggesting that it might play a role in survival and apoptosis of all cell types.
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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.