ArticleProceedings of the National Academy of Sciences of the United States of America2007
Molecular basis of MAPK-activated protein kinase 2:p38 assembly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
What it found
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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.
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Who cites it
53 citing papers in PubMed, 110 citations in OpenAlex.
- Structural and dynamic insights into the allosteric activation of p38α MAP kinase via specific docking interactions.Communications biology · 2026Article
- Targeting of kinases to treat neurodegenerative diseases.Pharmacological reviews · 2026Review
- MK2/p38/p53 Suppress Basal IL-1β and Non-Canonical NF-κB Signaling in Macrophages.International journal of molecular sciences · 2026Article
- Non-Catalytic Inhibitors of the p38/MK2 Interface: Repurposing Approved Drugs to Target Neuroinflammation in Alzheimer's Disease.Journal of medicinal chemistry · 2025Article
- MK2 nonenzymatically promotes nuclear translocation of caspase-3 and resultant apoptosis.American journal of physiology. Lung cellular and molecular physiology · 2023Article
- Article
- Mitogen-activated protein kinase-activated protein kinase-2 (MK2) and its role in cell survival, inflammatory signaling, and migration in promoting cancer.Molecular carcinogenesis · 2022Article
- Decisive role of water and protein dynamics in residence time of p38α MAP kinase inhibitors.Nature communications · 2022Article
- MK2 degradation as a sensor of signal intensity that controls stress-induced cell fate.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The interaction of p38 with its upstream kinase MKK6.Protein science : a publication of the Protein Society · 2021Article
- Prevention of Melanoma Extravasation as a New Treatment Option Exemplified by p38/MK2 Inhibition.International journal of molecular sciences · 2020Article
- MAP Kinase-Mediated Activation of RSK1 and MK2 Substrate Kinases.Structure (London, England : 1993) · 2020Article
- A Dynamic Switch in Inactive p38γ Leads to an Excited State on the Pathway to an Active Kinase.Biochemistry · 2019Article
- Structural Insight into the 14-3-3 Protein-dependent Inhibition of Protein Kinase ASK1 (Apoptosis Signal-regulating kinase 1).The Journal of biological chemistry · 2016Article
- Targeting Mitogen-Activated Protein Kinase-Activated Protein Kinase 2 (MAPKAPK2, MK2): Medicinal Chemistry Efforts To Lead Small Molecule Inhibitors to Clinical Trials.Journal of medicinal chemistry · 2016Review
- GTPase domain driven dimerization of SEPT7 is dispensable for the critical role of septins in fibroblast cytokinesis.Scientific reports · 2016Article
- p38 MAP kinases in the heart.Gene · 2016Review
- Article
- Pivotal Role of Mitogen-Activated Protein Kinase-Activated Protein Kinase 2 in Inflammatory Pulmonary Diseases.Current protein & peptide science · 2016Review
- Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p38 MAPK and MAPK-activated protein kinase 2 (MK2) are key components of signaling pathways leading to many cellular responses, notably the proinflammatory cytokine production. The physical association of p38alpha isoform and MK2 is believed to be physiologically important for this signaling. We report the 2.7-A resolution crystal structure of the unphosphorylated complex between p38alpha and MK2. These protein kinases bind "head-to-head," present their respective active sites on approximately the same side of the heterodimer, and form extensive intermolecular interactions. Among these interactions, the MK2 Ile-366-Ala-390, which includes the bipartite nuclear localization signal, binds to the p38alpha-docking region. This binding supports the involvement of noncatalytic regions to the tight binding of the MK2:p38alpha binary assembly. The MK2 residues 345-365, containing the nuclear export signal, block access to the p38alpha active site. Some regulatory phosphorylation regions of both protein kinases engage in multiple interactions with one another in this complex. This structure gives new insights into the regulation of the protein kinases p38alpha and MK2, aids in the better understanding of their known cellular and biochemical studies, and provides a basis for understanding other regulatory protein-protein interactions involving signal transduction proteins.
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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.