ArticleJournal of the American Chemical Society2011
Resting and active states of the ERK2:HePTP complex.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 31 citations in OpenAlex.
- Hydrogen peroxide-dependent oxidation of ERK2 within its D-recruitment site alters its substrate selection.iScience · 2023Article
- Structural insights into Acyl-coenzyme A binding domain containing 3 (ACBD3) protein hijacking by picornaviruses.Protein science : a publication of the Protein Society · 2019Article
- Molecular basis for the binding and selective dephosphorylation of NaNature communications · 2019Article
- Recent Advances in Coarse-Grained Models for Biomolecules and Their Applications.International journal of molecular sciences · 2019Review
- Membrane fluctuations and acidosis regulate cooperative binding of 'marker of self' protein CD47 with the macrophage checkpoint receptor SIRPα.Journal of cell science · 2018Article
- Structures of Dynamic Protein Complexes: Hybrid Techniques to Study MAP Kinase Complexes and the ESCRT System.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Slow inhibition and conformation selective properties of extracellular signal-regulated kinase 1 and 2 inhibitors.Biochemistry · 2015Article
- Structure and dynamics of a compact state of a multidomain protein, the mercuric ion reductase.Biophysical journal · 2014Article
- Phosphorylation releases constraints to domain motion in ERK2.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Interaction of kinase-interaction-motif protein tyrosine phosphatases with the mitogen-activated protein kinase ERK2.PloS one · 2014Article
- Molecular mechanism of ERK dephosphorylation by striatal-enriched protein tyrosine phosphatase.Journal of neurochemistry · 2014Article
- 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
- The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study.Structure (London, England : 1993) · 2013Article
- Protein tyrosine phosphatases: structure, function, and implication in human disease.Methods in molecular biology (Clifton, N.J.) · 2013Review
- A CC-SAM, for coiled coil-sterile α motif, domain targets the scaffold KSR-1 to specific sites in the plasma membrane.Science signaling · 2012Article
- Docking interactions of hematopoietic tyrosine phosphatase with MAP kinases ERK2 and p38α.Biochemistry · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The MAP kinase ERK2 (ERK2, extracellular signal-regulated kinase 2) is regulated by numerous phosphatases that tightly control its activity. For example, the hematopoietic tyrosine phosphatase (HePTP) negatively regulates T cell activation in lymphocytes via ERK2 dephosphorylation. However, only very limited structural information is available for these biologically important complexes. Here, we use small-angle X-ray scattering combined with EROS ensemble refinement to characterize the structures of the resting and active states of ERK2:HePTP complexes. Our data show that the resting state ERK2:HePTP complex adopts a highly extended, dynamic conformation that becomes compact and ordered in the active state complex. This work experimentally demonstrates that these complexes undergo significant dynamic structural changes in solution and provides the first structural insight into an active state MAPK complex.
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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.