ArticleInternational journal of molecular sciences2018
In-Cell NMR Study of Tau and MARK2 Phosphorylated Tau.
Article in International journal of molecular sciences, 2018. 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, 31 citations in OpenAlex.
- Metal Binding to Tau Protein: Physiological and Pathological Relevance.Biochemistry · 2026Review
- Genome-wide association studies reveal a functional SNP and candidate genes associated with alkali tolerance in alfalfa.Plant molecular biology · 2026Article
- In-Cell Residue-Resolved NMR of Micromolar α-Synuclein and Tau at 310 K.Journal of the American Chemical Society · 2025Article
- Genome-wide identification of peanut ERFs and functional characterization of AhERF28 in response to salt and drought stresses.Plant cell reports · 2025Article
- Stability of the polarization agent AsymPolPOK in intact and lysed mammalian cells.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025Article
- Stability of the polarization agent AsymPolPOK in intact and lysed mammalian cells.bioRxiv : the preprint server for biology · 2024Article
- Role of MARK2 in the nervous system and cancer.Cancer gene therapy · 2024Review
- Deciphering the functional roles of transporter proteins in subcellular metal transportation of plants.Planta · 2023Review
- Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression.Communications biology · 2022Article
- Tau Toxicity in Neurodegeneration.Molecular neurobiology · 2022Review
- Radio Signals from Live Cells: The Coming of Age of In-Cell Solution NMR.Chemical reviews · 2022Review
- In-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells.Journal of the American Chemical Society · 2021Article
- Studying protein folding in health and disease using biophysical approaches.Emerging topics in life sciences · 2021Article
- NMR Studies of Tau Protein in Tauopathies.Frontiers in molecular biosciences · 2021Review
- Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2019Article
- In-Cell NMR: Analysis of Protein-Small Molecule Interactions, Metabolic Processes, and Protein Phosphorylation.International journal of molecular sciences · 2019Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The intrinsically disordered protein, Tau, is abundant in neurons and contributes to the regulation of the microtubule (MT) and actin network, while its intracellular abnormal aggregation is closely associated with Alzheimer's disease. Here, using in-cell Nuclear Magnetic Resonance (NMR) spectroscopy, we investigated the conformations of two different isoforms of Tau, Tau40 and k19, in mammalian cells. Combined with immunofluorescence imaging and western blot analyses, we found that the isotope-enriched Tau, which was delivered into the cultured mammalian cells by electroporation, is partially colocalized with MT and actin filaments (F-actin). We acquired the NMR spectrum of Tau in human embryonic kidney 293 (HEK-293T) cells, and compared it with the NMR spectra of Tau added with MT, F-actin, and a variety of crowding agents, respectively. We found that the NMR spectrum of Tau in complex with MT best recapitulates the in-cell NMR spectrum of Tau, suggesting that Tau predominantly binds to MT at its MT-binding repeats in HEK-293T cells. Moreover, we found that disease-associated phosphorylation of Tau was immediately eliminated once phosphorylated Tau was delivered into HEK-293T cells, implying a potential cellular protection mechanism under stressful conditions. Collectively, the results of our study reveal that Tau utilizes its MT-binding repeats to bind MT in mammalian cells and highlight the potential of using in-cell NMR to study protein structures at the residue level in mammalian cells.
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