ArticlePloS one2014
Thermodynamics of the interaction between Alzheimer's disease related tau protein and DNA.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 41 citations in OpenAlex.
- Tau condensation on DNA mediates microtubule attachment suggesting a mitotic role for centromere-localized tau.Nature communications · 2026Article
- Phosphorylation regulates tau's phase separation behavior and interactions with chromatin.Communications biology · 2024Article
- Phosphorylation regulates tau's phase separation behavior and interactions with chromatin.bioRxiv : the preprint server for biology · 2023Article
- Dendrimers and Derivatives as Multifunctional Nanotherapeutics for Alzheimer's Disease.Pharmaceutics · 2023Review
- Importin-Mediated Pathological Tau Nuclear Translocation Causes Disruption of the Nuclear Lamina, TDP-43 Mislocalization and Cell Death.Frontiers in molecular neuroscience · 2022Article
- Mechanisms of secretion and spreading of pathological tau protein.Cellular and molecular life sciences : CMLS · 2020Review
- β-Amyloid Peptide: the Cell Compartment Multi-faceted Interaction in Alzheimer's Disease.Neurotoxicity research · 2020Review
- Nuclear Transport Deficits in Tau-Related Neurodegenerative Diseases.Frontiers in neurology · 2020Review
- Kinetic and thermodynamic study of beta-Boswellic acid interaction with Tau protein investigated by surface plasmon resonance and molecular modeling methods.BioImpacts : BI · 2020Article
- High specificity of widely used phospho-tau antibodies validated using a quantitative whole-cell based assay.Journal of neurochemistry · 2020Article
- It's all about tau.Progress in neurobiology · 2019Review
- Spreading of α-Synuclein and Tau: A Systematic Comparison of the Mechanisms Involved.Frontiers in molecular neuroscience · 2019Review
- Tau Biology, Tauopathy, Traumatic Brain Injury, and Diagnostic Challenges.Journal of Alzheimer's disease : JAD · 2019Review
- Frontotemporal Dementia-Associated N279K Tau Mutation Localizes at the Nuclear Compartment.Frontiers in cellular neuroscience · 2018Article
- Roles of tau protein in health and disease.Acta neuropathologica · 2017Review
- Loss of Tau protein affects the structure, transcription and repair of neuronal pericentromeric heterochromatin.Scientific reports · 2016Article
- An evolutionary roadmap to the microtubule-associated protein MAP Tau.BMC genomics · 2016Article
- Nuclear Tau and Its Potential Role in Alzheimer's Disease.Biomolecules · 2016Review
- Tau Structures.Frontiers in aging neuroscience · 2016Review
- A Simple Model to Study Tau Pathology.Journal of experimental neuroscience · 2016Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tau hyperphosphorylation can be considered as one of the hallmarks of Alzheimer's disease and other tauophaties. Besides its well-known role as a microtubule associated protein, Tau displays a key function as a protector of genomic integrity in stress situations. Phosphorylation has been proven to regulate multiple processes including nuclear translocation of Tau. In this contribution, we are addressing the physicochemical nature of DNA-Tau interaction including the plausible influence of phosphorylation. By means of surface plasmon resonance (SPR) we measured the equilibrium constant and the free energy, enthalpy and entropy changes associated to the Tau-DNA complex formation. Our results show that unphosphorylated Tau binding to DNA is reversible. This fact is in agreement with the protective role attributed to nuclear Tau, which stops binding to DNA once the insult is over. According to our thermodynamic data, oscillations in the concentration of dephosphorylated Tau available to DNA must be the variable determining the extent of Tau binding and DNA protection. In addition, thermodynamics of the interaction suggest that hydrophobicity must represent an important contribution to the stability of the Tau-DNA complex. SPR results together with those from Tau expression in HEK cells show that phosphorylation induces changes in Tau protein which prevent it from binding to DNA. The phosphorylation-dependent regulation of DNA binding is analogous to the Tau-microtubules binding inhibition induced by phosphorylation. Our results suggest that hydrophobicity may control Tau location and DNA interaction and that impairment of this Tau-DNA interaction, due to Tau hyperphosphorylation, could contribute to Alzheimer's pathogenesis.
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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.