ArticleBiochemistry2012
Docking interactions of hematopoietic tyrosine phosphatase with MAP kinases ERK2 and p38α.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 19 citations in OpenAlex.
- Structural and dynamic insights into the allosteric activation of p38α MAP kinase via specific docking interactions.Communications biology · 2026Article
- Hydrogen peroxide-dependent oxidation of ERK2 within its D-recruitment site alters its substrate selection.iScience · 2023Article
- Proteome-wide screening for mitogen-activated protein kinase docking motifs and interactors.Science signaling · 2023Article
- Structural basis for the recognition of the bacterial tyrosine kinase Wzc by its cognate tyrosine phosphatase Wzb.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The methylJournal of biomolecular NMR · 2020Article
- 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
- Specificity of Phosphorylation Responses to Mitogen Activated Protein (MAP) Kinase Pathway Inhibitors in Melanoma Cells.Molecular & cellular proteomics : MCP · 2018Article
- 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
- Structural and Dynamic Features of F-recruitment Site Driven Substrate Phosphorylation by ERK2.Scientific reports · 2015Article
- Allosteric enhancement of MAP kinase p38α's activity and substrate selectivity by docking interactions.Nature structural & molecular biology · 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
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Hematopoietic tyrosine phosphatase (HePTP) regulates orthogonal MAP kinase signaling cascades by dephosphorylating both extracellular signal-regulated kinase (ERK) and p38. HePTP recognizes a docking site (D-recruitment site, DRS) on its targets using a conserved N-terminal sequence motif (D-motif). Using solution nuclear magnetic resonance spectroscopy and isothermal titration calorimetry, we compare, for the first time, the docking interactions of HePTP with ERK2 and p38α. Our results demonstrate that ERK2-HePTP interactions primarily involve the D-motif, while a contiguous region called the kinase specificity motif also plays a key role in p38α-HePTP interactions. D-Motif-DRS interactions for the two kinases, while similar overall, do show some specific differences.
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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.