ArticleMolecular biology of the cell2016
Presence of a carboxy-terminal pseudorepeat and disease-like pseudohyperphosphorylation critically influence tau's interaction with microtubules in axon-like processes.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
31 citing papers in PubMed, 61 citations in OpenAlex.
- Article
- Beyond microtubule regulation: the multifaceted roles of tau in neuronal function and dysfunction.Translational psychiatry · 2026Review
- Application of modular isoxazoline-βiScience · 2025Article
- Quantitative live cell imaging of a tauopathy model enables the identification of a polypharmacological drug candidate that restores physiological microtubule interaction.Nature communications · 2024Article
- Tau, microtubule dynamics, and axonal transport: New paradigms for neurodegenerative disease.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Insights into the Structural Conformations of the Tau Protein in Different Aggregation Status.Molecules (Basel, Switzerland) · 2023Review
- Site-Specific C-Terminal Fluorescent Labeling of Tau Protein.ACS omega · 2022Article
- Super-resolution imaging and quantitative analysis of microtubule arrays in model neurons show that epothilone D increases the density but decreases the length and straightness of microtubules in axon-like processes.Brain research bulletin · 2022Article
- Microtubule-binding core of the tau protein.Science advances · 2022Article
- Caspase-cleaved tau is senescence-associated and induces a toxic gain of function by putting a brake on axonal transport.Molecular psychiatry · 2022Article
- What's in a Gene? The Outstanding Diversity ofCells · 2022Review
- Genetic Screening in Korean Patients with Frontotemporal Dementia Syndrome.Journal of Alzheimer's disease reports · 2022Article
- Microtubule-modulating Agents in the Fight Against Neurodegeneration: Will it ever Work?Current neuropharmacology · 2022Review
- Tau Post-Translational Modifications: Potentiators of Selective Vulnerability in Sporadic Alzheimer's Disease.Biology · 2021Review
- Phosphorylated tau targeted small-molecule PROTACs for the treatment of Alzheimer's disease and tauopathies.Biochimica et biophysica acta. Molecular basis of disease · 2021Review
- Dendritic/Post-synaptic Tau and Early Pathology of Alzheimer's Disease.Frontiers in molecular neuroscience · 2021Review
- Analysis of Genotype-Phenotype Correlations in Patients With Degenerative Dementia Through the Whole Exome Sequencing.Frontiers in aging neuroscience · 2021Article
- The Crosstalk Between Pathological Tau Phosphorylation and Mitochondrial Dysfunction as a Key to Understanding and Treating Alzheimer's Disease.Molecular neurobiology · 2020Review
- The physiological roles of tau and Aβ: implications for Alzheimer's disease pathology and therapeutics.Acta neuropathologica · 2020Review
- Much More Than a Cytoskeletal Protein: Physiological and Pathological Functions of the Non-microtubule Binding Region of Tau.Frontiers in neurology · 2020Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A current challenge of cell biology is to investigate molecular interactions in subcellular compartments of living cells to overcome the artificial character of in vitro studies. To dissect the interaction of the neuronal microtubule (MT)-associated protein tau with MTs in axon-like processes, we used a refined fluorescence decay after photoactivation approach and single-molecule tracking. We found that isoform variation had only a minor influence on the tau-MT interaction, whereas the presence of a C-terminal pseudorepeat region (PRR) greatly increased MT binding by a greater-than-sixfold reduction of the dissociation rate. Bioinformatic analysis revealed that the PRR contained a highly conserved motif of 18 amino acids. Disease-associated tau mutations in the PRR (K369I, G389R) did not influence apparent MT binding but increased its dynamicity. Simulation of disease-like tau hyperphosphorylation dramatically diminished the tau-MT interaction by a greater-than-fivefold decrease of the association rate with no major change in the dissociation rate. Apparent binding of tau to MTs was similar in axons and dendrites but more sensitive to increased phosphorylation in axons. Our data indicate that under the conditions of high MT density that prevail in the axon, tau's MT binding and localization are crucially affected by the presence of the PRR and tau hyperphosphorylation.
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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.