Near-atomic model of microtubule-tau interactions
Open accessPublished version of a preprint
Abstract
Tackling microtubule-tau interactions: Alzheimer's disease is a major cause of death in the elderly. Disease progression is associated with the accumulation of neurofibrillary tangles composed of tau, a protein important for neuronal development and function. Tangle formation is preceded by phosphorylation events that cause tau to dissociate from its native binding partner, microtubules. Microtubule-tau interactions have been mysterious. Kellogg et al. used cryo–electron microscopy and molecular modeling to show how tau interacts with the outer surface of the microtubule, stapling together tubulin subunits and thus stabilizing the polymer. A key tau amino acid within the tightly bound segment between tubulin subunits corresponds to a clinically relevant site of tau phosphorylation, explaining the competition between microtubule interaction and tau aggregation. Science , this issue p. 1242
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Such regional variation is consistent with previous studies and suggests that lattice conformation can be locally influenced by lattice-binding microtubule-associated proteins, post-translational modifications, mechanical stress, or repair processes.
“Such regional variation is consistent with previous studies58and suggest that lattice conformation can be locally influenced by lattice-binding microtuble-associated proteins (MAPs)59–61, post-translational modifications, mechanical stress50,51, or repair processes62–66.”
From Ghost Neuron preparation unlocks high-resolution structural mapping of intracellular architecture in axons (2026) · cites this paper as [59]
Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measuredTau's function and microtubule affinity are modulated by alternative splicing and phosphorylation.
“Tau’s function and microtubule affinity are modulated by alternative splicing (Kellogg et al., 2018; McVicker et al., 2014) and phosphorylation, both of which play key roles in normal development and pathology”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Kellogg et al., 2018
MAP4 adopts a conformation completely distinct from that of tau on microtubules, which may at least partially explain why MAP4 is unable to form envelopes.
“MAP4 adopts a conformation completely distinct from that of tau41,44 on microtubules, which may at least partially explain why, unlike tau, MAP4 is unable to form envelopes.”
From Microtubule lattice spacing governs cohesive envelope formation of tau family proteins (2022) · cites this paper as [41]
Tau promotes the polymerization and stability of microtubules.
“As a microtubule binding component, tau promotes the polymerization and stability of microtubules [119–121].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [121]
Tau phosphorylation at specific sites overlapping AD sites diminishes tau's affinity for microtubules.
“It is well established that tau phosphorylation, especially at specific sites that overlap with the sites that are phosphorylated in AD, diminishes the affinity of tau for microtubules (4, 26–29).”
From All the Tau We Cannot See (2023) · cites this paper as [28]
Pathological tau protein is in a highly phosphorylated state and is cleaved abnormally, resulting in an abnormal conformation and aggregation, which leads to neurofibrillary tauopathies.
“Pathological tau protein is in a highly phosphorylated state and is cleaved abnormally, resulting in an abnormal conformation and aggregation, which leads to neurofibrillary tauopathies [18,19,20].”
From Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review (2024) · cites this paper as [19]
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- Authors
- Kellogg, E. H., Hejab, N. M. A., Poepsel, S., Downing, K. H., DiMaio, F., & Nogales, E.
- Affiliations
- Lawrence Berkeley National Laboratory (US)
- QB3 (US)
- University of Washington (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Nogales, Eva
- Venue
- Science
- Published
- 2018-06-15
- Volume
- 360
- Issue
- 6394
- Pages
- 1242-1246
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC6225777
- OpenAlex
- W2800724568
- Cited by
- 416
- References
- 48
- Citations by year
- 2026: 44 · 2025: 44 · 2024: 33 · 2023: 56 · 2022: 48 · 2021: 47 · 2020: 63 · 2019: 64 · 2018: 17
- FWCI
- 32.74
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Locations
- Science (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- NIH Office of the Director (GM123089, GM051487)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- tau protein, microtubules, tau hyperphosphorylation, microtubule stabilization, protofilaments, Alzheimer's disease, cryo-electron microscopy, atomic models
- MeSH terms
- Humans, Microtubules, Models, Chemical, Phosphorylation, Phylogeny, tau Proteins, Conserved Sequence, Tandem Repeat Sequences, Cryoelectron Microscopy, Polymerization
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