ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structural assembly of the signaling competent ERK2-RSK1 heterodimeric protein kinase complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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, 38 citations in OpenAlex.
- A conserved dimerization element is required for protein kinase activation bybioRxiv : the preprint server for biology · 2026Article
- Structural insights and biophysical characterization of p90RSK2:ERK2 complex.The Biochemical journal · 2025Article
- RiSKs in Computational Modeling of Isoform-Selective RSK Inhibitors.Journal of chemical information and modeling · 2025Review
- Phosphorylation-Assisted Luciferase Complementation Assay Designed to Monitor Kinase Activity and Kinase-Domain-Mediated Protein-Protein Binding.International journal of molecular sciences · 2023Article
- Article
- Activation and inhibition of the C-terminal kinase domain of p90 ribosomal S6 kinases.Life science alliance · 2023Article
- A non-catalytic herpesviral protein reconfigures ERK-RSK signaling by targeting kinase docking systems in the host.Nature communications · 2022Article
- The functional regulatory details of ERK2 in complex with RSK1: anRSC advances · 2021Article
- Inhibition of SNCG suppresses the proliferation of lung cancer cells induced by high glucose.Molecular medicine reports · 2021Article
- MAP Kinase-Mediated Activation of RSK1 and MK2 Substrate Kinases.Structure (London, England : 1993) · 2020Article
- Emerging roles of the αC-β4 loop in protein kinase structure, function, evolution, and disease.IUBMB life · 2020Review
- Targeting ERK beyond the boundaries of the kinase active site in melanoma.Molecular carcinogenesis · 2019Review
- Evolution of a dynamic molecular switch.IUBMB life · 2019Review
- Disordered Protein Kinase Regions in Regulation of Kinase Domain Cores.Trends in biochemical sciences · 2019Review
- Rewiring of RSK-PDZ Interactome by Linear Motif Phosphorylation.Journal of molecular biology · 2019Article
- Dimethyl fumarate is an allosteric covalent inhibitor of the p90 ribosomal S6 kinases.Nature communications · 2018Article
- Structural insights into ubiquitin phosphorylation by PINK1.Scientific reports · 2018Article
- Phenotypic Characterization of a Comprehensive Set of MAPK1/ERK2 Missense Mutants.Cell reports · 2016Article
- Structural Basis of Ribosomal S6 Kinase 1 (RSK1) Inhibition by S100B Protein: MODULATION OF THE EXTRACELLULAR SIGNAL-REGULATED KINASE (ERK) SIGNALING CASCADE IN A CALCIUM-DEPENDENT WAY.The Journal of biological chemistry · 2016Article
- Systematic discovery of linear binding motifs targeting an ancient protein interaction surface on MAP kinases.Molecular systems biology · 2015Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
Mitogen-activated protein kinases (MAPKs) bind and activate their downstream kinase substrates, MAPK-activated protein kinases (MAPKAPKs). Notably, extracellular signal regulated kinase 2 (ERK2) phosphorylates ribosomal S6 kinase 1 (RSK1), which promotes cellular growth. Here, we determined the crystal structure of an RSK1 construct in complex with its activator kinase. The structure captures the kinase-kinase complex in a precatalytic state where the activation loop of the downstream kinase (RSK1) faces the enzyme's (ERK2) catalytic site. Molecular dynamics simulation was used to show how this heterodimer could shift into a signaling-competent state. This structural analysis combined with biochemical and cellular studies on MAPK→MAPKAPK signaling showed that the interaction between the MAPK binding linear motif (residing in a disordered kinase domain extension) and the ERK2 "docking" groove plays the major role in making an encounter complex. This interaction holds kinase domains proximal as they "readjust," whereas generic kinase domain surface contacts bring them into a catalytically competent state.
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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.