Tau co-organizes dynamic microtubule and actin networks
Open accessAbstract
The crosstalk between microtubules and actin is essential for cellular functions. However, mechanisms underlying the microtubule-actin organization by cross-linkers remain largely unexplored. Here, we report that tau, a neuronal microtubule-associated protein, binds to microtubules and actin simultaneously, promoting in vitro co-organization and coupled growth of both networks. By developing an original assay to visualize concomitant microtubule and actin assembly, we show that tau can induce guided polymerization of actin filaments along microtubule tracks and growth of single microtubules along actin filament bundles. Importantly, tau mediates microtubule-actin co-alignment without changing polymer growth properties. Mutagenesis studies further reveal that at least two of the four tau repeated motifs, primarily identified as tubulin-binding sites, are required to connect microtubules and actin. Tau thus represents a molecular linker between microtubule and actin networks, enabling a coordination of the two cytoskeletons that might be essential in various neuronal contexts.
AI snapshot
Written from the paper’s full text.
TL;DR
Tau binds microtubules and F-actin simultaneously and acts as a molecular linker that co-organizes dynamic microtubule and actin networks in vitro. At least two of tau’s four repeat motifs are required for this cross-linking, while coupled growth does not alter the intrinsic elongation rates of either polymer.
Key findings
- Recombinant 4R-tau bound F-actin with an apparent Kd of 241 ± 43 nM, close to its Kd for microtubules (280 ± 52 nM), and bundled F-actin without significantly changing actin assembly or elongation speed (1.78 ± 0.28 vs. 1.76 ± 0.41 μm/min for control vs. tau).
- In a live TIRF co-assembly assay, tau induced guided polymerization of actin along microtubule tracks and growth of microtubules along actin bundles; up to 60% of the microtubule network co-aligned with F-actin, versus no more than 14% with fascin.
- Co-alignment did not change growth rates: microtubules grew at 1.28 ± 0.17 μm/min alone (n = 52) and 1.31 ± 0.16 μm/min when co-aligned with actin (n = 41); F-actin along microtubules grew at 1.21 ± 0.16 μm/min (n = 80) versus 1.29 ± 0.29 μm/min for isolated actin (n = 35).
- Tau mutants with 2, 3, or 4 repeats gave about 50% microtubule–actin co-alignment, whereas 1R- and 0R-tau almost abolished cross-linking, indicating that at least two repeat motifs are needed to bridge the polymers.
Methods
- In vitro reconstituted cell-free assays using purified recombinant human tau isoforms and mutants, bovine brain tubulin, rabbit skeletal muscle actin, fascin, and profilin.
- Binding and bundling were measured by co-sedimentation, light scattering, low-speed sedimentation, and fluorescence microscopy; dynamic co-organization was visualized by dual-color TIRF microscopy with simultaneous tubulin and actin polymerization.
- Image analysis used ImageJ and custom macros/kymographs to quantify microtubule–actin overlap, elongation rates, and F-actin curvature; statistics were performed in Prism 6.
Limitations
- The paper states that whether and how phosphorylation sites in or near tau’s repeats modulate F-actin affinity and microtubule/actin cross-linking “remain to be elucidated.”
- The study is entirely in vitro using reconstituted cell-free systems; no cellular or in vivo validation of the proposed linker function is presented.
- The text makes evident that tubulin and tau concentrations/ratios were adjusted for different tau constructs to synchronize polymerization and avoid excessive microtubule nucleation, so the reconstituted conditions may not reflect physiological concentrations.
Model-written summary. Check it against the paper before relying on it.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
3 of 13 cited sources checked · 2 supported · 0 flagged · accuracy not yet measured
- Findingown data
The percentage of the microtubule surface associated with actin filaments in the presence of 1R- and 0R-tau strongly decreased to values comparable to those obtained with fascin.
“In these conditions, the percentage of the microtubule surface associated with actin filaments strongly decreased to values comparable to those obtained with fascin (Fig. 3b).”
Quote in the paperSubstantial claim - Findingown data
Tau promotes the appearance of bundled F-actin in a concentration-dependent manner.
“tau influenced actin organization by promoting the apparition of bundled F-actin in a concentration dependent manner, as revealed by light scattering (Fig. 1d) and low-speed sedimentation assays (Fig. 1e, see also Supplementary Fig. S1f).”
Quote in the paperSubstantial claim - Findingown data
Tau mediates microtubule-actin co-alignment.
“tau mediates microtubule-actin co-alignment without changing polymer growth properties”
- Also stated in: § Tau coordinates dynamic microtubules and actin filaments · plain
“tau promotes the co-alignment of microtubules and actin filaments”
- Also stated in: § Tau simultaneously binds to microtubules and actin filaments · plain
“hybrid bundles of co-aligned microtubules and actin filaments appeared in the presence of tau”
Quote in the paperSubstantial claim - Also stated in: § Tau coordinates dynamic microtubules and actin filaments · plain
- Findingown data
ΔN-tau cross-links both polymers in growing conditions similarly to full-length tau.
“and cross-links both polymers in growing conditions similarly to the full-length tau (Fig. 3b, Supplementary Movie S5).”
Quote in the paperSubstantial claim - Findingown data
Tau does not significantly affect actin assembly properties.
“We found that tau did not significantly affect actin assembly properties by using pyrene-actin polymerization and F-actin sedimentation (Supplementary Fig. S1d and e).”
Quote in the paperNot a substantial claim
- Findingown data
Tau binds microtubules with an apparent equilibrium dissociation constant (Kdapp) of about 280 ± 52 nM.
“a value close to Kdapp of tau for microtubules measured by a similar experimental approach (280 ± 52 nM, Fig. 1b)”
Quote in the paperSubstantial claim - Findingown data
In the absence of tau, single microtubules and F-actin are randomly distributed in solution.
“In the absence of tau, single microtubules and F-actin were randomly distributed in the solution (Fig. 1h, left)”
Quote in the paperSubstantial claim - Findingown data
Tau promotes in vitro co-organization of microtubule and actin networks.
“Here, we report that tau, a neuronal microtubule-associated protein, binds to microtubules and actin simultaneously, promoting in vitro co-organization and coupled growth of both networks.”
- Also stated in: § Tau coordinates dynamic microtubules and actin filaments · plain
“tau was able to coordinate microtubule and actin networks by progressively co-aligning growing microtubules and growing actin filaments”
Quote in the paperSubstantial claim - Also stated in: § Tau coordinates dynamic microtubules and actin filaments · plain
- Findingown data
In the presence of fascin, the proportion of the microtubule network associated with F-actin does not exceed 14%.
“whereas it did not exceed 14% in the presence of fascin (Fig. 2g).”
Quote in the paperSubstantial claim - Findingown data
Tau induces guided polymerization of actin filaments along microtubule tracks.
“tau can induce guided polymerization of actin filaments along microtubule tracks”
- Also stated in: § Tau coordinates dynamic microtubules and actin filaments · plain
“guided polymerization of single or bundled actin filaments along single or bundled microtubule tracks”
Quote in the paperSubstantial claim - Also stated in: § Tau coordinates dynamic microtubules and actin filaments · plain
- Findingown data
ΔN-tau binds to F-actin and microtubules independently.
“Our results show that ΔN-tau binds to F-actin and to microtubules independently (Supplementary Fig. S2b and c)”
Quote in the paperSubstantial claim - Findingown data
Tau does not change polymer growth properties during microtubule-actin co-alignment.
“tau mediates microtubule-actin co-alignment without changing polymer growth properties”
- Also stated in: § Tau coordinates dynamic microtubules and actin filaments · plain
“the tight association and coupled growth of microtubules and F-actin did not modify the intrinsic assembly properties of each polymer”
Quote in the paperSubstantial claim - Also stated in: § Tau coordinates dynamic microtubules and actin filaments · plain
- Findingown data
Tau binds to microtubules and actin simultaneously.
“Here, we report that tau, a neuronal microtubule-associated protein, binds to microtubules and actin simultaneously, promoting in vitro co-organization and coupled growth of both networks.”
- Also stated in: § Tau simultaneously binds to microtubules and actin filaments · hedged
“suggesting that tau simultaneously interacts with both cytoskeletons and promotes the formation of large macro-molecular complexes.”
Quote in the paperSubstantial claim - Also stated in: § Tau simultaneously binds to microtubules and actin filaments · hedged
- Findingown data
Tau binds F-actin with an apparent equilibrium dissociation constant (Kdapp) of about 241 ± 43 nM.
“Our results showed that tau bound to actin filaments (F-actin) with an apparent equilibrium dissociation constant (Kdapp) of about 241 ± 43 nM (Fig. 1c)”
Quote in the paperSubstantial claim - Findingown data
In the presence of tau, the proportion of the microtubule network associated with F-actin increases up to 60% as a function of the total microtubule surface.
“the proportion of the microtubule network associated with F-actin increases up to 60% as a function of the total microtubule surface”
Quote in the paperSubstantial claim - Findingown data
In the presence of tau proteins with 2, 3 and 4 repeats, about 50% of the microtubule network co-aligned with actin filaments.
“In the presence of tau proteins with 2, 3 and 4 repeats, about 50% of the microtubule network co-aligned with actin filaments.”
Quote in the paperSubstantial claim - Findingown data
Deletion of more than two repeats (1R- and 0R-tau) almost abolished the link between the two cytoskeletal arrays.
“In contrast, the deletion of more than two repeats (1R- and 0R-tau) almost abolished the link between the two cytoskeletal arrays (Fig. 3b,c).”
Quote in the paperSubstantial claim - Findingown data
The elongation rate of F-actin polymerizing along microtubule tracks is similar to that of isolated actin filaments.
“The elongation rate of F-actin polymerizing along microtubule tracks (1.21 ± 0.16 μm/min, n = 80) was also very similar to the one measured for isolated actin filaments (1.29 ± 0.29 μm/min, n = 35).”
Quote in the paperSubstantial claim - Findingown data
The different deleted forms of tau still associated independently with microtubules and F-actin in similar concentration ratios used for the TIRF assay.
“The different deleted forms of tau still associated independently with microtubules and F-actin in similar concentration ratios of tubulin:tau and actin:tau used for the TIRF assay (Supplementary Fig. S2b and c).”
Quote in the paperSubstantial claim - Findingown data
Microtubule speed does not change when microtubule-growing ends encounter actin filaments and co-align.
“Measurements of growth rates indicated that the microtubule speed (1.28 ± 0.17 μm/min, n = 52) did not change when microtubule-growing ends encountered actin filaments and co-aligned (1.31 ± 0.16 μm/min, n = 41).”
Quote in the paperSubstantial claim - Findingown data
Tau does not significantly change the elongation speed of actin compared to control.
“Quantification of actin growth rate at early time points indicated that tau did not significantly changed the elongation speed of actin compared to the control (1.78 ± 0.28 and 1.76 ± 0.41 μm/min, respectively).”
Quote in the paperSubstantial claim - Findingown data
Tau induces growth of single microtubules along actin filament bundles.
“growth of single microtubules along actin filament bundles”
- Also stated in: § Tau coordinates dynamic microtubules and actin filaments · plain
“We also observed the growth of single microtubules along F-actin cables”
Quote in the paperSubstantial claim - Also stated in: § Tau coordinates dynamic microtubules and actin filaments · plain
- Findingown data
The Kdapp value of tau for F-actin is similar in the buffers used for actin assembly and actin/tubulin co-assembly.
“The Kdapp value of tau for F-actin was similar in the buffers used either for actin assembly (Fig. 1c) or actin/tubulin co-assembly (Supplementary Fig. S1c).”
Quote in the paperNot a substantial claim - Findingown data
Tau promotes coupled growth of microtubule and actin networks in vitro.
“Here, we report that tau, a neuronal microtubule-associated protein, binds to microtubules and actin simultaneously, promoting in vitro co-organization and coupled growth of both networks.”
- Also stated in: § Discussion · boosted
“Our work demonstrates that tau acts as a molecular linker between microtubules and actin filaments, enabling the in vitro co-organization and coupled growth of the two networks (Fig. 4).”
Quote in the paperSubstantial claim - Also stated in: § Discussion · boosted
- Premisecitation
Tau has been found on dynamic microtubules in the actin-rich growth cone areas of developing neurons.
“Tau has also been found on dynamic microtubules in the actin-rich growth cone areas of developing neurons2425.”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [2425]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- Interpretationown data
At least two of the four tau repeated motifs are required to connect microtubules and actin.
“at least two of the four tau repeated motifs, primarily identified as tubulin-binding sites, are required to connect microtubules and actin”
- Also stated in: § Tau bridges microtubules and actin via its tubulin-binding sites · hedged
“Our results suggest a mechanism whereby a minimum of two tau repeats are required to bridge polymers”
Quote in the paperSubstantial claim - Also stated in: § Tau bridges microtubules and actin via its tubulin-binding sites · hedged
- Interpretationown data
The repeat motifs are crucial for the microtubule/actin cross-linking activity of tau.
“These data indicate that the repeat motifs are crucial for the microtubule/actin cross-linking activity of tau.”
Quote in the paperSubstantial claim - Interpretationown data
The C-terminal part of tau is sufficient to establish a physical link between microtubules and actin filaments.
“This suggests that the C-terminal part of tau is sufficient to establish a physical link between microtubules and actin filaments”
Quote in the paperSubstantial claim - Interpretationown data
These data provide the first evidence for a direct role of tau in the dynamic coordination of microtubule and actin cytoskeletons.
“These data provide the first evidence for a direct role of tau in the dynamic coordination of microtubule and actin cytoskeletons.”
Quote in the paperSubstantial claim - Interpretationown data
Tau dimerization through its N-terminal part is unlikely involved in microtubule/actin cross-linking.
“and that tau dimerization through its N-terminal part is unlikely involved in this process.”
Quote in the paperSubstantial claim - Premisecitation
Tau is implicated in the regulation of the actin cytoskeleton.
“Beyond its microtubule-stabilizing properties, tau is also implicated in the regulation of actin cytoskeleton16.”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [16] Griffiths, L. M. & Pollards, D. The Interaction of Actin Filaments with Microtubules and Microtubule- associated Proteins. J. Biol. Chem. 257, 9143–9151 (1982). source
- Premisecitation
Tau neurotoxicity correlates with alterations of actin organization in animal models of Alzheimer's disease.
“Furthermore, tau neurotoxicity correlates with alterations of actin organization in animal models of Alzheimer’s disease17.”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [17] Fulga, T. a. et al. Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo. Nat. Cell Biol. 9, 139–48 (2007). source
- Classified as probably not a substantial claim. 3
- May combine two claims. 8
Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
PremisecitationSeveral in vitro studies have reported the association with actin of full-length tau and tau sub-regions containing the microtubule-binding sites, although this direct interaction has been controverted.
“Accordingly, several in vitro studies have reported the association with actin of the full-length tau1718 and tau sub-regions containing the microtubule-binding sites1920, although this direct interaction has been controverted21.”
Quote in the paperNot a substantial claim1 of 3 sources checked- cites [1718]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- cites [1920]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- cites [21] Roger, B., Al-Bassam, J., Dehmelt, L., Milligan, R & Halpain, S. MAP2c, but not tau, binds and bundles F-actin via its microtubule binding domain. Curr. Biol. 14, 363–71 (2004). source
May combine two claims.
PremisecitationIn vivo, tau co-localizes with actin in differentiating PC12 cells and in the post-synaptic compartments of mature neurons.
“In vivo, tau co-localizes with actin in differentiating PC12 cells22 and in the post-synaptic compartments of mature neurons23.”
Quote in the paperSubstantial claim1 of 2 sources checked- cites [22] Yu, J.-Z. & Rasenick, M. M. Tau associates with actin in differentiating PC12 cells. FASEB J. 20, 1452–61 (2006). source
- cites [23] Frandemiche, M. L. et al. Activity-dependent tau protein translocation to excitatory synapse is disrupted by exposure to amyloid-beta oligomers. J. Neurosci. 34, 6084–97 (2014). source
Citation 23 attaches to the postsynaptic-neuron part of the sentence, not the PC12-cell part. Figure 4 shows tau and F-actin colocalizing in dendritic spines of cultured cortical neurons after synaptic activation, while Figure 1 reports only limited colocalization under resting conditions. These cell-culture observations do not establish the claim's in vivo setting. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Classified as probably not a substantial claim. May combine two claims.
PremisecitationThe interaction of tau with microtubules in neurons is well documented and more recent studies have proposed that tau also binds to actin.
“The interaction of tau with microtubules in neurons is well documented and more recent studies have proposed that tau also binds to actin34.”
Quote in the paperSubstantial claim1 of 1 sources checked- cites [34] Morris, M., Maeda, S., Vossel, K. & Mucke, L. The many faces of tau. Neuron 70, 410–26 (2011). source
May combine two claims.
Findingown dataFascin induces cross-linking of actin filaments but neither affects microtubule organization nor promotes microtubule/actin interactions.
“Addition of fascin, a specific actin-bundler29, induced cross-linking of actin filaments, but neither affected microtubule organization nor promoted microtubule/actin interactions (Fig. 2a, Supplementary Movie S2).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [29] Edwards, R. A. & Bryan, J. Fascins, a family of actin bundling proteins. Cell. Motil. Cytoskeleton 32, 1–9 (1995). source
Classified as probably not a substantial claim. May combine two claims.
PremisecitationTau is a neuronal microtubule-associated protein that promotes microtubule polymerization and bundling and is responsible for microtubule stabilization in axons.
“Tau is a neuronal microtubule-associated protein that promotes microtubule polymerization and bundling7891011, and is responsible for microtubule stabilization in axons1213.”
Quote in the paperSubstantial claim0 of 2 sources checked- cites 7891011
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- cites [1213]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
May combine two claims.
Interpretationown dataTau is a molecular linker between microtubule and actin networks, enabling in vitro co-organization and coupled growth of the two networks.
“Tau thus represents a molecular linker between microtubule and actin networks, enabling a coordination of the two cytoskeletons that might be essential in various neuronal contexts.”
- Also stated in: § Discussion · boosted
“Our work demonstrates that tau acts as a molecular linker between microtubules and actin filaments, enabling the in vitro co-organization and coupled growth of the two networks (Fig. 4).”
Quote in the paperSubstantial claim- Also stated in: § Discussion · boosted
May combine two claims.
Premiseown dataOverall, these data support a role for tau as a regulator of microtubules and actin, and suggest that tau is a potential linker between the two cytoskeletons.
“Overall, these data support a role for tau as a regulator of microtubules and actin, and suggest that tau is a potential linker between the two cytoskeletons as hypothesized some years ago1.”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [1] Rodriguez, O. C. et al. Conserved microtubule – actin interactions in cell movement and morphogenesis. Nat. Cell. Biol. 5, 599–609 (2003). source
May combine two claims.
Interpretationown dataA minimum of two tau repeats are required to bridge polymers, with one repeat bound to microtubules and the other one to actin filaments.
“Our results suggest a mechanism whereby a minimum of two tau repeats are required to bridge polymers, with one repeat bound to microtubules and the other one to actin filaments (Fig. 4).”
Quote in the paperSubstantial claim
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The difference between the measured Tau/F-actin dissociation constant and the previously reported value is likely due to differences in ionic strength.
“This is likely due of differences in ionic strength, because previous studies used phosphate buffer7, while we chose general actin assembly buffer.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [7]
The Methods section ('Tau interaction with microtubules or F-actin'; page unavailable) says the cited study measured Tau/F-actin binding in AP (actin-polymerization) buffer, not phosphate buffer. The Results section ('Tau simultaneously binds to microtubules and actin filaments'; page unavailable) reports the dissociation constant but does not attribute a difference from a previously reported value to ionic strength. (LLM, conf=0.85)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredThis result supports recent in vitro evidence that Tau can induce guided polymerization of Actin filaments along microtubule tracks.
“This result supports recent in vitro evidence that Tau can induce guided polymerization of Actin filaments along microtubule tracks [27, 68].”
From Expression of Tau Produces Aberrant Plasma Membrane Blebbing in Glial Cells Through RhoA-ROCK-Dependent F-Actin Remodeling (2016) · cites this paper as [27]
The derived dissociation constant for Tau/F-actin is lower than the previously reported value of 241 ± 43 nM.
“The derived dissociation constant is lower than a previously reported value of 241 ± 43 nM7.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [7]
MAPs bundle actin filaments and cross-link the cellular cytoskeleton formed by microtubules and actin filaments.
“In addition, MAPs bundle actin filaments and cross-link the cellular cytoskeleton formed by microtubules and actin filaments (Fig. 1a)3–10.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [7]
Tau binds in vitro simultaneously to microtubules and actin filaments.
“Consistent with these findings in cells, Tau binds in vitro simultaneously to microtubules and actin filaments7.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [7]
Experimentally observed cross-linking of microtubules and actin filaments by Tau.
“in agreement with experimentally observed cross-linking of microtubules and actin filaments by Tau7.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [7]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
Actin fluorophore differs between methods descriptions
MinorThe protein-purification section says actin was labelled with Alexa-568 or pyrene, but the actin-polymerization assay specifies Alexa-468-labelled actin. The described fluorophore is inconsistent.
“Actin was purified from rabbit skeletal muscle and labelled with Alexa-568 or pyrene43.”
“Actin growth was initiated by flowing 0.4 μM G-actin (containing 30% Alexa-468 labelled G-actin) together with 0.1 μM 4R-tau”
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Self-citationGlucose Regulates Microtubule Disassembly and the Dose of Insulin Secretion via Tau Phosphorylation
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Self-citationSeptins mediate a microtubule–actin crosstalk that enables actin growth on microtubules
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- Authors
- Elie, A., Prezel, E., Guérin, C., Denarier, E., Ramirez-Rios, S., Serre, L., Andrieux, A., Fourest-Lieuvin, A., Blanchoin, L., & Arnal, I.
- Affiliations
- Inserm (FR)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Arnal, Isabelle
- Venue
- Scientific Reports
- Published
- 2015-05-05
- Volume
- 5
- Issue
- 1
- Pages
- 9964-9964
- ISSN
- 2045-2322 (ISSN-L)
- PMC
- PMC4421749
- OpenAlex
- W1803223003
- Semantic Scholar
- ceed83152f677f0df838603cde88006d92c6924b
- Cited by
- 200
- References
- 49
- Citations by year
- 2026: 14 · 2025: 16 · 2024: 17 · 2023: 11 · 2022: 18 · 2021: 27 · 2020: 26 · 2019: 27 · 2018: 16 · 2017: 15 · 2016: 12
- FWCI
- 7.62
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Scientific Reports (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Funders
- Agence Nationale de la Recherche (MALZ 2011)
- Institut National de la Santé et de la Recherche Médicale
- Fondation pour la Recherche Médicale
- Ministère de l'Enseignement Supérieur et de la Recherche
- Centre National de la Recherche Scientifique
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- tau protein, tubulin binding site, neuronal cytoskeleton
- MeSH terms
- Actins, Binding Sites, Cross-Linking Reagents, Actin Cytoskeleton, Microtubules, Motion, Protein Binding, Protein Conformation, tau Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Claims read by deepseek-v4.1-flash under definition version 3 (extract-v3) on 2026-11-02.
Classified by jev-1.13-20260917 (gold-guideline-v0.2) on 2026-11-02.
Cited sources are checked by gpt-6-sol.
Statistics and arithmetic are recomputed, not judged.
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