ArticleStructure (London, England : 1993)2013
The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Coordinated differentiation of human intestinal organoids with functional enteric neurons and vasculature.Cell stem cell · 2025Article
- Comprehensive analysis ofFrontiers in genetics · 2022Article
- The interaction of p38 with its upstream kinase MKK6.Protein science : a publication of the Protein Society · 2021Article
- The methylJournal of biomolecular NMR · 2020Article
- The expression patterns and the diagnostic/prognostic roles of PTPN family members in digestive tract cancers.Cancer cell international · 2020Article
- Dynamics of transcriptome changes during subcutaneous preadipocyte differentiation in ducks.BMC genomics · 2019Article
- The KIM-family protein-tyrosine phosphatases use distinct reversible oxidation intermediates: Intramolecular or intermolecular disulfide bond formation.The Journal of biological chemistry · 2017Article
- Role of Striatal-Enriched Tyrosine Phosphatase in Neuronal Function.Neural plasticity · 2016Review
- Protein tyrosine phosphatases as potential therapeutic targets.Acta pharmacologica Sinica · 2014Review
- 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
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The MAP kinase p38α is essential for neuronal signaling. To better understand the molecular regulation of p38α we used atomistic and molecular techniques to determine the structural basis of p38α regulation by the two neuronal tyrosine phosphatases, PTPSL/PTPBR7 (PTPRR) and STEP (PTPN5). We show that, despite the fact that PTPSL and STEP belong to the same family of regulatory proteins, they interact with p38α differently and their distinct molecular interactions explain their different catalytic activities. Although the interaction of PTPSL with p38α is similar to that of the previously described p38α:HePTP (PTPN7) complex, STEP binds and regulates p38α in an unexpected manner. Using NMR and small-angle X-ray scattering data, we generated a model of the p38α:STEP complex and define molecular differences between its resting and active states. Together, these results provide insights into molecular regulation of p38α by key regulatory proteins.
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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.