ArticleThe Journal of biological chemistry2016
Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated Kinase.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 65 citations in OpenAlex.
- Article
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- Spatial differences in gene expression across the dorsal raphe nucleus in a model of early Alzheimer's disease.Journal of Alzheimer's disease : JAD · 2025Article
- GSK3β phosphorylation catalyzes the aggregation of tau into Alzheimer's disease-like filaments.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Pleiotropic Associations with Alzheimer's Disease and Physical Activity: Sex Differences and the Effects of Environment.International journal of molecular sciences · 2024Article
- Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review.Molecules (Basel, Switzerland) · 2024Review
- Article
- The Role of Traditional Chinese Medicine Natural Products in β-Amyloid Deposition and Tau Protein Hyperphosphorylation in Alzheimer's Disease.Drug design, development and therapy · 2023Review
- Alterations in Cerebellar Microtubule Cytoskeletal Network in a ValproicAcid-Induced Rat Model of Autism Spectrum Disorders.Biomedicines · 2022Article
- Neuroprotective Action of Coumarin Derivatives through Activation of TRKB-CREB-BDNF Pathway and Reduction of Caspase Activity in Neuronal Cells Expressing Pro-Aggregated Tau Protein.International journal of molecular sciences · 2022Article
- Alzheimer's disease: Ablating single master site abolishes tau hyperphosphorylation.Science advances · 2022Article
- Structural Basis for Chaperone-Independent Ubiquitination of Tau Protein by Its E3 Ligase CHIP.Angewandte Chemie (International ed. in English) · 2022Article
- Aging and high-fat diet feeding lead to peripheral insulin resistance and sex-dependent changes in brain of mouse model of tau pathology THY-Tau22.Journal of neuroinflammation · 2021Article
- Mutant Presenilin 1 Dysregulates Exosomal Proteome Cargo Produced by Human-Induced Pluripotent Stem Cell Neurons.ACS omega · 2021Article
- Alterations in Tau Protein Level and Phosphorylation State in the Brain of the Autistic-Like Rats Induced by Prenatal Exposure to Valproic Acid.International journal of molecular sciences · 2021Article
- The structure and phase of tau: from monomer to amyloid filament.Cellular and molecular life sciences : CMLS · 2021Review
- Flavonoids as an Intervention for Alzheimer's Disease: Progress and Hurdles Towards Defining a Mechanism of Action.Brain plasticity (Amsterdam, Netherlands) · 2021Review
- Novel Synthetic Coumarin-Chalcone Derivative (E)-3-(3-(4-(Dimethylamino)Phenyl)Acryloyl)-4-Hydroxy-2Oxidative medicine and cellular longevity · 2021Article
- NMR Studies of Tau Protein in Tauopathies.Frontiers in molecular biosciences · 2021Review
- Modification of lipid rafts by extracellular vesicles carrying HIV-1 protein Nef induces redistribution of amyloid precursor protein and Tau, causing neuronal dysfunction.The Journal of biological chemistry · 2020Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Tau neuronal protein has a central role in neurodegeneration and is implicated in Alzheimer disease development. Abnormal phosphorylation of Tau impairs its interaction with other proteins and is associated with its dysregulation in pathological conditions. Molecular mechanisms leading to hyperphosphorylation of Tau in pathological conditions are unknown. Here, we characterize phosphorylation of Tau by extracellular-regulated kinase (ERK2), a mitogen-activated kinase (MAPK) that responds to extracellular signals. Analysis ofin vitrophosphorylated Tau by activated recombinant ERK2 with nuclear magnetic resonance spectroscopy (NMR) reveals phosphorylation of 15 Ser/Thr sites.In vitrophosphorylation of Tau using rat brain extract and subsequent NMR analysis identifies the same sites. Phosphorylation with rat brain extract is known to transform Tau into an Alzheimer disease-like state. Our results indicate that phosphorylation of Tau by ERK2 alone is sufficient to produce the same characteristics. We further investigate the mechanism of ERK2 phosphorylation of Tau. Kinases are known to recognize their protein substrates not only by their specificity for a targeted Ser or Thr phosphorylation site but also by binding to linear-peptide motifs called docking sites. We identify two main ERK2 docking sites in Tau sequence using NMR. Our results suggest that ERK2 dysregulation in Alzheimer disease could lead to abnormal phosphorylation of Tau resulting in the pathology of the disease.
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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.