ArticleCell death and differentiation2012
A critical step for JNK activation: isomerization by the prolyl isomerase Pin1.
Article in Cell death and differentiation, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026Review
- Covalent Inhibition of the Peptidyl-Prolyl Isomerase Pin1 by Sulfopin Results in a Broad Impact on the Phosphoproteome of Human Osteosarcoma U2-OS Cells.Proteomics · 2025Article
- Pin1-catalyzed conformational regulation after phosphorylation: A distinct checkpoint in cell signaling and drug discovery.Science signaling · 2024Review
- The molecular mechanisms of peptidyl-prolylFrontiers in pharmacology · 2024Review
- Cyclophilin A Isomerisation of Septin 2 Mediates Abscission during Cytokinesis.International journal of molecular sciences · 2023Article
- Regulation of eukaryotic protein kinases by Pin1, a peptidyl-prolyl isomerase.Advances in biological regulation · 2023Article
- Neuronal Signaling Involved in Neuronal Polarization and Growth: Lipid Rafts and Phosphorylation.Frontiers in molecular neuroscience · 2020Article
- Review
- FAF1 mediates necrosis through JNK1-mediated mitochondrial dysfunction leading to retinal degeneration in the ganglion cell layer upon ischemic insult.Cell communication and signaling : CCS · 2018Article
- Pin1 Modulation in Physiological Status and Neurodegeneration. Any Contribution to the Pathogenesis of Type 3 Diabetes?International journal of molecular sciences · 2018Review
- Profiling Subcellular Protein Phosphatase Responses to Coxsackievirus B3 Infection of Cardiomyocytes.Molecular & cellular proteomics : MCP · 2017Article
- Novel Insights into the PKCβ-dependent Regulation of the Oxidoreductase p66Shc.The Journal of biological chemistry · 2016Article
- Proline isomerisation as a novel regulatory mechanism for p38MAPK activation and functions.Cell death and differentiation · 2016Article
- Physiological and Pathogenic Roles of Prolyl Isomerase Pin1 in Metabolic Regulations via Multiple Signal Transduction Pathway Modulations.International journal of molecular sciences · 2016Review
- The isomerase PIN1 controls numerous cancer-driving pathways and is a unique drug target.Nature reviews. Cancer · 2016Review
- cJun N-terminal kinase (JNK) phosphorylation of serine 36 is critical for p66Shc activation.Scientific reports · 2016Article
- Dipeptidyl peptidase 4 promotes epithelial cell transformation and breast tumourigenesis via induction of PIN1 gene expression.British journal of pharmacology · 2015Article
- Pin1-mediated Sp1 phosphorylation by CDK1 increases Sp1 stability and decreases its DNA-binding activity during mitosis.Nucleic acids research · 2014Article
- Prolyl isomerase Pin1 in cancer.Cell research · 2014Review
- Pin1: a molecular orchestrator in the heart.Trends in cardiovascular medicine · 2014Review
Corrections and comments
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Authors and funding
10 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
c-Jun N-terminal kinase (JNK) is activated by dual phosphorylation of both threonine and tyrosine residues in the phosphorylation loop of the protein in response to several stress factors. However, the precise molecular mechanisms for activation after phosphorylation remain elusive. Here we show that Pin1, a peptidyl-prolyl isomerase, has a key role in the JNK1 activation process by modulating a phospho-Thr-Pro motif in the phosphorylation loop. Pin1 overexpression in human breast cancer cell lines correlates with increased JNK activity. In addition, small interfering RNA (siRNA) analyses showed that knockdown of Pin1 in a human breast cancer cell line decreased JNK1 activity. Pin1 associates with JNK1, and then catalyzes prolyl isomerization of the phospho-Thr-Pro motif in JNK1 from trans- to cis-conformation. Furthermore, Pin1 enhances the association of JNK1 with its substrates. As a result, Pin1(-/-) cells are defective in JNK activation and resistant to oxidative stress. These results provide novel insights that, following stress-induced phosphorylation of Thr in the Thr-Pro motif of JNK1, JNK1 associates with Pin1 and undergoes conformational changes to promote the binding of JNK1 to its substrates, resulting in cellular responses from extracellular signals.
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