ArticleBiochemistry2011
Solution NMR insights into docking interactions involving inactive ERK2.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 44 citations in OpenAlex.
- Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Linear motif specificity in signaling through p38α and ERK2 mitogen-activated protein kinases.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Hydrogen peroxide-dependent oxidation of ERK2 within its D-recruitment site alters its substrate selection.iScience · 2023Article
- Identification and biochemical characterization of small molecule inhibitors of ERK2 that target the D-recruitment site.Methods in enzymology · 2023Article
- Development of small molecule extracellular signal-regulated kinases (ERKs) inhibitors for cancer therapy.Acta pharmaceutica Sinica. B · 2022Review
- ERK signalling: a master regulator of cell behaviour, life and fate.Nature reviews. Molecular cell biology · 2020Review
- Modulating multi-functional ERK complexes by covalent targeting of a recruitment site in vivo.Nature communications · 2019Article
- Targeting ERK beyond the boundaries of the kinase active site in melanoma.Molecular carcinogenesis · 2019Review
- Functional divergence caused by mutations in an energetic hotspot in ERK2.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- A Novel Class of Common Docking Domain Inhibitors That Prevent ERK2 Activation and Substrate Phosphorylation.ACS chemical biology · 2019Article
- Endogenous, regulatory cysteine sulfenylation of ERK kinases in response to proliferative signals.Free radical biology & medicine · 2017Article
- Local destabilization, rigid body, and fuzzy docking facilitate the phosphorylation of the transcription factor Ets-1 by the mitogen-activated protein kinase ERK2.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- NMR Characterization of Information Flow and Allosteric Communities in the MAP Kinase p38γ.Scientific reports · 2016Article
- Identification of inhibitors that target dual-specificity phosphatase 5 provide new insights into the binding requirements for the two phosphate pockets.BMC biochemistry · 2015Article
- Article
- Structural and Dynamic Features of F-recruitment Site Driven Substrate Phosphorylation by ERK2.Scientific reports · 2015Article
- Quantification of a Pharmacodynamic ERK End Point in Melanoma Cell Lysates: Toward Personalized Precision Medicine.ACS medicinal chemistry letters · 2015Article
- Molecular basis of MAP kinase regulation.Protein science : a publication of the Protein Society · 2013Review
- Structural basis for the regulation of the mitogen-activated protein (MAP) kinase p38α by the dual specificity phosphatase 16 MAP kinase binding domain in solution.The Journal of biological chemistry · 2013Article
- Structural mechanism for the specific assembly and activation of the extracellular signal regulated kinase 5 (ERK5) module.The Journal of biological chemistry · 2013Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
The mitogen-activated protein (MAP) kinase ERK2 contains recruitment sites that engage canonical and noncanonical motifs found in a variety of upstream kinases, regulating phosphatases and downstream targets. Interactions involving two of these sites, the D-recruitment site (DRS) and the F-recruitment site (FRS), have been shown to play a key role in signal transduction by ERK/MAP kinases. The dynamic nature of these recruitment events makes NMR uniquely suited to provide significant insight into these interactions. While NMR studies of kinases in general have been greatly hindered by their large size and complex dynamic behavior leading to the suboptimal performance of standard methodologies, we have overcome these difficulties for inactive full-length ERK2 and obtained an acceptable level of backbone resonance assignments. This allowed a detailed investigation of the structural perturbations that accompany interactions involving both canonical and noncanonical recruitment events. No crystallographic information exists for the latter. We found that the chemical shift perturbations in inactive ERK2, indicative of structural changes in the presence of canonical and noncanonical motifs, are not restricted to the recruitment sites but also involve the linker that connects the N- and C-lobes and, in most cases, a gatekeeper residue that is thought to exert allosteric control over catalytic activity. We also found that, even though the canonical motifs interact with the DRS utilizing both charge-charge and hydrophobic interactions, the noncanonical interactions primarily involve the latter. These results demonstrate the feasibility of solution NMR techniques for a comprehensive analysis of docking interactions in a full-length ERK/MAP kinase.
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Registered trials
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