ArticleBiophysical journal2009
Human microtubule-associated-protein tau regulates the number of protofilaments in microtubules: a synchrotron x-ray scattering study.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 81 citations in OpenAlex.
- Tau physiology and pathology: impacts on cellular structures and neurodegenerative diseases.Inflammopharmacology · 2026Review
- ENKD1 Modulates Skin Elasticity Through Microtubule Stability Regulation.Cytoskeleton (Hoboken, N.J.) · 2026Article
- The N-terminal domain of COMPANION OF CELLULOSE SYNTHASE1 promotes microtubule array formation in Arabidopsis.Plant physiology · 2025Article
- Mixtures of Intrinsically Disordered Neuronal Protein Tau and Anionic Liposomes Reveal Distinct Anionic Liposome-Tau Complexes Coexisting with Tau Liquid-Liquid Phase Separated Coacervates.bioRxiv : the preprint server for biology · 2024Article
- Complexes of tubulin oligomers and tau form a viscoelastic intervening network cross-bridging microtubules into bundles.Nature communications · 2024Article
- Prion-like strain effects in tauopathies.Cell and tissue research · 2023Review
- Probing the existence of non-thermal Terahertz radiation induced changes of the protein solution structure.Scientific reports · 2021Article
- Microtubule Dysfunction: A Common Feature of Neurodegenerative Diseases.International journal of molecular sciences · 2020Review
- The Role of Copper in Tau-Related Pathology in Alzheimer's Disease.Frontiers in molecular neuroscience · 2020Review
- Minireview - Microtubules and Tubulin Oligomers: Shape Transitions and Assembly by Intrinsically Disordered Protein Tau and Cationic Biomolecules.Langmuir : the ACS journal of surfaces and colloids · 2019Review
- Dynamic behaviors of α-synuclein and tau in the cellular context: New mechanistic insights and therapeutic opportunities in neurodegeneration.Neurobiology of disease · 2019Review
- Dynamical decoration of stabilized-microtubules by Tau-proteins.Scientific reports · 2019Article
- Coherent diffractive imaging of microtubules using an X-ray laser.Nature communications · 2019Article
- Article
- A Closer Look into the Role of Protein Tau in the Identification of Promising Therapeutic Targets for Alzheimer's Disease.Brain sciences · 2018Review
- Microtubule Hyperacetylation Enhances KL1-Dependent Micronucleation under a Tau Deficiency in Mammary Epithelial Cells.International journal of molecular sciences · 2018Article
- On the Origin of Microtubules' High-Pressure Sensitivity.Biophysical journal · 2018Article
- Tau can switch microtubule network organizations: from random networks to dynamic and stable bundles.Molecular biology of the cell · 2018Article
- Alpha-synuclein facilitates to form short unconventional microtubules that have a unique function in the axonal transport.Scientific reports · 2017Article
- Tau antagonizes end-binding protein tracking at microtubule ends through a phosphorylation-dependent mechanism.Molecular biology of the cell · 2016Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
Microtubules (MTs), a major component of the eukaryotic cytoskeleton, are 25 nm protein nanotubes with walls comprised of assembled protofilaments built from alphabeta heterodimeric tubulin. In neural cells, different isoforms of the microtubule-associated-protein (MAP) tau regulate tubulin assembly and MT stability. Using synchrotron small angle x-ray scattering (SAXS), we have examined the effects of all six naturally occurring central nervous system tau isoforms on the assembly structure of taxol-stabilized MTs. Most notably, we found that tau regulates the distribution of protofilament numbers in MTs as reflected in the observed increase in the average radius R(MT) of MTs with increasing Phi, the tau/tubulin-dimer molar ratio. Within experimental scatter, the change in R(MT) seems to be isoform independent. Significantly, R(MT) was observed to rapidly increase for 0 < Phi < 0.2 and saturate for Phi between 0.2-0.5. Thus, a local shape distortion of the tubulin dimer on tau binding, at coverages much less than a monolayer, is spread collectively over many dimers on the scale of protofilaments. This implies that tau regulates the shape of protofilaments and thus the spontaneous curvature C(o)(MT) of MTs leading to changes in the curvature C(MT) (=1/R(MT)). An important biological implication of these findings is a possible allosteric role for tau where the tau-induced shape changes of the MT surface may effect the MT binding activity of other MAPs present in neurons. Furthermore, the results, which provide insight into the regulation of the elastic properties of MTs by tau, may also impact biomaterials applications requiring radial size-controlled nanotubes.
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Registered trials
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