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Aβ Oligomers Cause Localized Ca 2+ Elevation, Missorting of Endogenous Tau into Dendrites, Tau Phosphorylation, and Destruction of Microtubules and Spines
Open accessAbstract
Aggregation of amyloid-β (Aβ) and Tau protein are hallmarks of Alzheimer's disease (AD), and according to the Aβ-cascade hypothesis, Aβ is considered toxic for neurons and Tau a downstream target of Aβ. We have investigated differentiated primary hippocampal neurons for early localized changes following exposure to Aβ oligomers. Initial events become evident by missorting of endogenous Tau into the somatodendritic compartment, in contrast to axonal sorting in normal neurons. In missorted dendritic regions there is a depletion of spines and local increase in Ca 2+ , and breakdown of microtubules. Tau in these regions shows elevated phosphorylation at certain sites diagnostic of AD-Tau (e.g., epitope of antibody 12E8, whose phosphorylation causes detachment of Tau from microtubules, and AT8 epitope), and local elevation of certain kinase activities (e.g., MARK/par-1, BRSK/SADK, p70S6K, cdk5, but not GSK3β, JNK, MAPK). These local effects occur without global changes in Tau, tubulin, or kinase levels. Somatodendritic missorting occurs not only with Tau, but also with other axonal proteins such as neurofilaments, and correlates with pronounced depletion of microtubules and mitochondria. The Aβ-induced effects on microtubule and mitochondria depletion, Tau missorting, and loss of spines are prevented by taxol, indicating that Aβ-induced microtubule destabilization and corresponding traffic defects are key factors in incipient degeneration. By contrast, the rise in Ca 2+ levels, kinase activities, and Tau phosphorylation cannot be prevented by taxol. Incipient and local changes similar to those of Aβ oligomers can be evoked by cell stressors (e.g., H 2 O 2 , glutamate, serum deprivation), suggesting some common mechanism of signaling.
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“mis-localization to dendrites and spines causing neurotoxicity [52]”
From Astrocytic APOE3-Christchurch expression ameliorates brain amyloid-β pathology in 5xFAD mice (2026) · cites this paper as [52]
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“Under normal conditions, tau is primarily localized to axons and promotes formation and stabilization of microtubules; however, in AD, tau becomes hyperphosphorylated and mislocalizes to somatodendritic compartments (Avila et al., 2004, Ittner et al., 2010, Zempel et al., 2010).”
From Dendritic Spine Remodeling and Synaptic Tau Levels in PS19 Tauopathy Mice (2021) · cites this paper as Zempel et al., 2010
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“the activities of two major tau kinases, GSK3 and PAR-1/microtubule affinity-regulating kinases (MARKs), are often associated with tau detachment from microtubules and Aβ-induced augmentation of tau toxicity [37, 39, 43–45].”
From Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity (2016) · cites this paper as [39]
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“Notably, studies in cultured neurons and transgenic Drosophila showed that Aβ-induced augmentation of tau toxicity caused by Aβ depends on tau phosphorylation at these sites [39, 45, 56–58].”
From Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity (2016) · cites this paper as [39]
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“Aβ promotes tau phosphorylation at disease-associated sites in in vitro and in vivo models of AD [2, 35–41].”
From Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity (2016) · cites this paper as [39]
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“In cellular and animal models, co-expression of Aβ augments tau phosphorylation at these sites and increases the levels of active GSK3 and PAR-1/MARK [2, 35–41, 43, 44].”
From Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity (2016) · cites this paper as [39]
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“Ab oligomers also cause tau mislocalization (77,78).”
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“Under normal conditions, tau is primarily localized to axons and promotes formation and stabilization of microtubules; however, in AD, tau becomes hyperphosphorylated and mislocalizes to somatodendritic compartments (Avila et al., 2004, Ittner et al., 2010, Zempel et al., 2010).”
From Dendritic Spine Remodeling and Synaptic Tau Levels in PS19 Tauopathy Mice (2021) · cites this paper as Zempel et al., 2010
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769 · cited 1×
“We also note that in our preparations we did not consistently observe a band at 56 kDa, a species that has been reported to be toxic for transgenic mice (Lesné et al., 2006) but can be visualized in certain conditions (Walsh et al., 2005; Ashe, 2006; Bernstein et al., 2009).”
BackgroundRetractedSoluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · cited 1×
“Despite numerous studies on the pathway of APP misprocessing and its consequences for neurons the modes of A toxicity have remained enigmatic (Haass and Selkoe, 2007; Small and Duff, 2008).”
BackgroundCommon structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · cited 1×
“Nevertheless, there were differences in structure because dot blots with antibody A11, which recognizes a more toxic generic amyloid conformation (Kayed et al., 2003), were more intense for F12 medium than for Nb (Fig.”
BackgroundDiffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506 · cited 3×
“There is a moderate decrease of ATP which is more apparent with F12 than with Nb medium, suggesting that F12, which was used in the original procedure (Lambert et al., 1998), could have some toxic effects on its own.”
BackgroundMethodTau-mediated neurodegeneration in Alzheimer’s disease and related disorders
Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174 · cited 1×
“These include loss of synapses and neurons, deficiency in neurotransmitters and metabolism, aggregation of amyloid- (A )-peptides into extracellular “amyloid plaques” and Tau protein into intracellular “neurofibrillary tangles” (Selkoe, 2004; Binder et al., 2005; Ballatore et al., 2007).”
BackgroundReducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model
Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892 · cited 1×
“…conversely Tau is considered necessary for the progression of neurodegeneration, as seen in cell and animal models (Rapoport et al., 2002; King et al., 2006; Roberson et al., 2007), and indeed the Tau pathology correlates well with clinical symptoms (Braak and Braak, 1991; Clavaguera et al., 2009).”
BackgroundTransmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803
Physiology and Pathophysiology of Purinergic Neurotransmission
Burnstock, G. (2007) · Physiological Reviews · doi:10.1152/physrev.00043.2006 · Cited by 1,609 · cited 1×
“We also tested extracellular ATP (100 M, 3 h), which functions as a stress signal and induces Ca 2 influx via P2 receptors and has been implicated in neurodegenerative disease (Burnstock, 2007).”
MethodShankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., & Sabatini, B. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4970-06.2007 · Cited by 1,592 · cited 1×
“4e,f), and involving NMDA receptors and others (De Felice et al., 2007; Shankar et al., 2007).”
BackgroundThe axonal transport of mitochondria
Saxton, W. M., & Hollenbeck, P. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.053850 · Cited by 1,218 · cited 1×
“As shown previously (Stamer et al., 2002; Hollenbeck and Saxton, 2005; Thies and Mandelkow, 2007), such mitochondrial traffic jams cause a local drop of energy (ATP) and consequently spine destruction through the perturbation of the actin network and loss of synaptic components (Whiteman et al.,…”
Background
Research works printed but not linked: 3
- 10.1242/jcs.02745 · DOI · Paper page
- 10.1074/jbc.R800036200 · DOI
- 10.1186/1750-1326-4-48 · DOI · Paper page
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Items 401–500 of 593
Monteiro‐Fernandes, D., Silva, J. M., Soares‐Cunha, C., Dalla, C., Kokras, N., Arnaud, F., Billiras, R., Zhuravleva, V., Waites, C. L., Bretin, S., et al. (2020) · Molecular Psychiatry · doi:10.1038/s41380-020-0794-5 · Cited by 20
Intraneuronal Tau Misfolding Induced by Extracellular Amyloid-β Oligomers
Rudenko, L. K., Wallrabe, H. K., Periasamy, A., Siller, K. H., Švindrych, Z., Seward, M. E., Best, M. N., & Bloom, G. S. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190226 · Cited by 24
Heme Oxygenase 1 Induces Tau Oligomer Formation and Synapse Aberrations in Hippocampal Neurons
Si, Z., Wang, X., Zhang, Z., Wang, J., Li, J., Li, J., Li, L., Li, Y., Peng, Y., Sun, C., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180451 · Cited by 24
Caballero, E., Calvo-Rodríguez, M., Gonzalo‐Ruiz, A., Villalobos, C., & Núñez, L. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.11.041 · Cited by 20
Epigenetic modulation of Cdk5 contributes to memory deficiency induced by amyloid fibrils
Li, L., Zhang, C., Zi, X., Tu, Q., & Guo, K. (2014) · Experimental Brain Research · doi:10.1007/s00221-014-4100-0 · Cited by 21
Proteomics of the astrocyte secretome reveals changes in their response to soluble oligomeric Aβ
Matafora, V., Gorb, A., Yang, F., Noble, W. J., Bachi, A., Perez‐Nievas, B. G., & Jiménez-Sánchez, M. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15875 · Cited by 19
Bell, M., Bachmann, S., Klimek, J., Langerscheidt, F., & Zempel, H. (2021) · Neuroscience · doi:10.1016/j.neuroscience.2021.01.041 · Cited by 34
Self-citationIndication of retrograde tau spreading along Braak stages and functional connectivity pathways
Seemiller, J., Bischof, G. N., Hoenig, M. C., Tahmasian, M., van Eimeren, T., Drzezga, A. E., & Initiative, A. T. A. D. N. (2021) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-020-05183-1 · Cited by 20
Targeting Tau to Treat Clinical Features of Huntington's Disease
Masnata, M., Salem, S., Jacquet, A. D. R., Anwer, M., & Cicchetti, F. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.580732 · Cited by 25
Liang, W., Zhang, W., Zhao, S.-F., Li, Q.-N., Liang, H., & Ceng, R. (2015) · Neurological Sciences · doi:10.1007/s10072-014-2014-z · Cited by 17
Rescue of tau-induced synaptic transmission pathology by paclitaxel
Erez, H., Shemesh, O. A., & Spira, M. E. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00034 · Cited by 22
“This conclusion is consistent with earlier biochemical studies of vertebrate neurons showing that tau-hyperphosphorylation and misfolding impair axoplasmic transport lead to depletion of essential molecular components at distal neuronal sites (Hall et al., 2001; Stamer et al., 2002; Coleman and Yao, 2003; Mandelkow et…”
ResultZempel, H., & Mandelkow, E. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6598-4_20 · Cited by 17
Self-citationDifferential vulnerability of hippocampal CA3-CA1 synapses to Aβ
Shipton, O. A., Tang, C. S., Paulsen, O., & Vargas‐Caballero, M. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01350-7 · Cited by 18
“The reduction in GluN2B subunit-containing NMDARmediated current could arise because Aβ increases tau phosphorylation [21], which in turn encourages aggregation of tau and its increased presence in the somatodendritic compartment [38].”
BackgroundDangerous Liaisons: Tau Interaction with Muscarinic Receptors
Wysocka, A., Pałasz, E., Steczkowska, M., & Niewiadomska, G. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666200424134311 · Cited by 24
Effect of Melatonin on Tau aggregation and Tau-mediated cell surface morphology
Das, R., Balmik, A., & Chinnathambi, S. (2019) · bioRxiv · doi:10.1101/861237 · Cited by 16
Fujiwara, H., Watanabe, S., Iwata, M., Ueda, S., Nobuhara, M., Wada-Kakuda, S., Misonou, H., & Miyasaka, T. (2019) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2019.10.191 · Cited by 16
Ectopic Expression Induces Abnormal Somatodendritic Distribution of Tau in the Mouse Brain
Kubo, A., Ueda, S., Yamane, A., Wada‐Kakuda, S., Narita, M., Matsuyama, M., Nomori, A., Takashima, A., Kato, T., Onodera, O., et al. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.2845-18.2019 · Cited by 17
“, 2014) and that the abnormal distribution of presumably unaggregated tau into dendrites or spines is a critical determinant for neurodegeneration (Zempel et al., 2010; Frandemiche et al., 2014).”
BackgroundModifying Rap1-signalling by targeting Pde6δ is neuroprotective in models of Alzheimer’s disease
Dumbacher, M., Dooren, T. V., Princen, K., Witte, K. D., Farinelli, M., Lievens, S., Tavernier, J. H., Dehaen, W., Wera, S., Winderickx, J., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0283-3 · Cited by 18
“Aberrant Ca signalling was shown to facilitate Tau phosphorylation [12] and Aβo production [13, 14], the precursors of the”
BackgroundSui, H., Zhang, L., Liu, Z., & Jin, Y. (2015) · Acta Pharmacologica Sinica · doi:10.1038/aps.2014.161 · Cited by 17
Regulation of Tau Homeostasis and Toxicity by Acetylation
Tracy, T. E., Claiborn, K. C., & Gan, L. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_4 · Cited by 17
Li, J.-Q., Ma, X.-H., Dai, H., Wang, C., Zhang, J., & Meng, X. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.119567 · Cited by 15
Amyloid-β in Alzheimer’s disease – front and centre after all?
Weglinski, C., & Jeans, A. F. (2022) · Neuronal Signaling · doi:10.1042/ns20220086 · Cited by 24
SIRT1 Regulates Tau Expression and Tau Synaptic Pathology
Yin, X., Zhou, Z., Qiu, Y., Fan, X., Zhao, C., Bao, J., Liu, C., Liu, F., & Qian, W. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215118 · Cited by 15
“Tau is hyperphosphorylated and mislocalizes to somatoden-dritic compartments in patient brain of AD [13, 69, 70].”
Dai, S.-Y., Zhou, F., Sun, J., & Li, Y. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210729 · Cited by 14
“This is consistent with Zempel H’s [35] finding that A (cid:2) may promote hyper phosphorylation of tau protein.”
Tripartite Relationship Among Synaptic, Amyloid, and Tau Proteins
Casaletto, K. B., Zetterberg, H., Blennow, K., Brinkmalm, A., Honer, W. G., Schneider, J. A., Bennett, D. A., Djukic, N. A., You, M. Y., Weiner‐Light, S., et al. (2021) · Neurology · doi:10.1212/wnl.0000000000012145 · Cited by 14
Polymorphic SERPINA3 prolongs oligomeric state of amyloid beta
Akbor, M. M., Kurosawa, N., Nakayama, H., Nakatani, A., Tomobe, K., Chiba, Y., Ueno, M., Tanaka, M., Nomura, Y., & Isobe, M. (2021) · PLoS ONE · doi:10.1371/journal.pone.0248027 · Cited by 17
“Oligomeric Aβ was found to be neurotoxic by activating N-methyl-D-aspartate receptors (NMDARs) induced excess calcium entry into neurons using Tg2576 AD model mice [51, 52].”
Harmonic Generation Microscopy 2.0: New Tricks Empowering Intravital Imaging for Neuroscience
Lim, H. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00099 · Cited by 20
“…modality offers new opportunities for investigating neurodegenerative disorders, such as Alzheimer’s disease and glaucoma, where disruption of axonal microtubules has been implicated (Matsuyama and Jarvik, 1989; Cash et al., 2003; Huang and Knighton, 2005; Huang et al., 2006; Zempel et al., 2010).”
BackgroundInvolvement of ‘stress–response’ kinase pathways in Alzheimer's disease progression
Mairet‐Coello, G., & Polleux, F. (2014) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2014.03.011 · Cited by 16
“For example, synthetic Ab oligomers or Ab dimers isolated from the brain of AD subjects induce hyperphosphorylation of Tau at AD-relevant epitopes in hippocampal neurons, Tau mislocalization into the somatodendritic compartment, disrupt the microtubule cytoskeleton and cause neuritic degeneration [9,69].”
BackgroundPark, S. S., Jung, H., Kim, Y., Park, T. K., Kim, C., Choi, H., Mook‐Jung, I. H., Koo, E. H., & Park, S. A. (2012) · Journal of Neurochemistry · doi:10.1111/jnc.12032 · Cited by 14
“2009) and mislocalization into dendritic spines, leading to a loss of spines and degeneration of dendrites (Zempel et al. 2010).”
BackgroundTau here, tau there, tau almost everywhere: Clarifying the distribution of tau in the adult CNS
Kanaan, N. M. (2024) · Cytoskeleton · doi:10.1002/cm.21820 · Cited by 15
“Several more recent studies report axon-specific localization of endogenous tau in cultured neurons (Bachmann et al., 2021; Balaji et al., 2018; Bell & Zempel, 2022; Li et al., 2011; Tjiang & Zempel, 2022; Zempel et al., 2010).”
BackgroundWang, L., Wei, Y., Sun, Z., Tai, W., Li, H., YaLing, Y., Jiang, L., & Wang, J. (2024) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14886 · Cited by 14
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“localization of tau to the dendrites [14] and mitochondria”
RetractedUntangling the role of tau in Alzheimer’s disease: A unifying hypothesis
Bhatia, N. S., & Hall, G. F. (2013) · Translational Neuroscience · doi:10.2478/s13380-013-0114-5 · Cited by 11
“The well-established dependence of Aβ-induced neurotoxicity on the presence of tau suggests that downstream neurodegenerative events appear to require the presence of a small but critical amount of somatodendritic, nonMT-associated tau [234-237], although it remains unclear whether this tau is derived from resident po…”
BackgroundCDK5 Targeting as a Therapy for Recovering Neurovascular Unit Integrity in Alzheimer’s Disease
Posada-Duque, R. A., & Cardona-Gómez, G. P. (2021) · Journal of Alzheimer's Disease · doi:10.3233/jad-200730 · Cited by 14
“At a fundamental level, complex AD pathology is based on aberrant Ca 2 + signaling, which leads to cell death [74–78].”
Anti-Correlated Cerebrospinal Fluid Biomarker Trajectories in Preclinical Alzheimer’s Disease
Gomar, J. J., Conejero-Goldberg, C., Davies, P., Goldberg, T. E., & Initiative, F. T. A. D. N. (2016) · Journal of Alzheimer’s Disease · doi:10.3233/jad-150937 · Cited by 13
“Additionally, both in vitro and preclinical work in transgenic mouse models of tau aggregation also suggests that A 42 may accelerate tau proto-aggregation or aggregation [38–40].”
BackgroundRNA‐Based Therapies for Neurodegenerative Diseases Targeting Pathogenic Proteins
Rabbani, S. A., El‐Tanani, M., Sharma, S., El‐Tanani, Y., Kumar, R., Saini, M., Yadav, M., Khan, M. A., & Parvez, S. (2025) · European Journal of Neuroscience · doi:10.1111/ejn.70110 · Cited by 15
“Additionally, synapse loss induced by exogenous application of Aβ in cultured neurons correlates with localized build-up of phosphorylated τ in dendrites (Zempel et al. 2010).”
KIBRA repairs synaptic plasticity and promotes resilience to tauopathy-related memory loss
Kauwe, G., Pareja-Navarro, K. A., Yao, L., Chen, J. H., Wong, I., Saloner, R., Cifuentes, H., Nana, A. L., Shah, S., Li, Y., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci169064 · Cited by 28
“…and synapse loss (8–10, 58, 59), but also dysregulation of axonal transport and axon initial segment function, as well as axon degeneration (60–62), altered mitochondrial bioenergetics (63), nuclear transport disruption (64, 65), altered proteostasis (66), and cytoskeletal destabilization (67, 68).”
Toxicities of amyloid-beta and tau protein are reciprocally enhanced in the Drosophila model
Sun, Z.-D., Hu, J.-X., Wu, J.-R., Zhou, B., & Hu, J. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.336872 · Cited by 14
“Subsequently, normal tau proteins are converted into hyperphosphorylated and pathological forms, leading to changes in tau localization, distribution, and aggregation (Zempel et al., 2010).”
Savioz, A., Giannakopoulos, P., Herrmann, F. R., Klein, W. L., Kövari, E., Bouras, C., & Giacobini, E. (2016) · Neurodegenerative Diseases · doi:10.1159/000446283 · Cited by 14
Microtubule-Tau Interaction as a Therapeutic Target for Alzheimer’s Disease
Ivashko‐Pachima, Y., Zhou, L.-Y., Lei, P., & Gozes, I. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0715-x · Cited by 15
Identification of novel Aβ-LilrB2 inhibitors as potential therapeutic agents for Alzheimer's disease
Lao, K., Zhang, R., Dai, Y., Luan, J., Guo, N., Xu, X., Zhang, Y., & Gou, X. (2021) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2021.103630 · Cited by 11
Interaction of Proteins Involved in Neuronal Proteinopathies
Kulichikhin, K. Y., Malikova, O. A., Zobnina, A. E., Zalutskaya, N. M., & Rubel, A. A. (2023) · Life · doi:10.3390/life13101954 · Cited by 17
Bartley, S. C., Proctor, M. T., Xia, H., Ho, E., Kang, D. S., Schuster, K. H., Bicca, M. A., Seckler, H. S., Viola, K. L., Patrie, S. M., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042208 · Cited by 14
“AD-related proteoforms of pTau, which are known to be upregulated by AβOs in cell and animal AD models [29,41,73], showed analogous patterns of expression.”
BackgroundAmyloid Metabolism and Amyloid-Targeting Blood-Based Biomarkers of Alzheimer’s Disease
Pyun, J., Kang, M. J., Ryoo, N., Suh, J., Youn, Y. C., Park, Y. H., & Kim, S. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200104 · Cited by 11
“A (cid:2) Os have been shown to be able to trigger tau pathology [33, 34], impair axonal transport [35], induce oxidative stress [26] and inflammation [36], and lead to cholinergic impairment [37], deteriorated synapses [19], and neuronal death [38].”
Chan, H. H., Koh, R. Y., Lim, C. L., & Leong, C. O. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666191023102422 · Cited by 15
Khan, R. I., Nirzhor, S. S. R., & Rashid, B. (2018) · Brain Sciences · doi:10.3390/brainsci8090162 · Cited by 12
RPS23RG1 reduces Aβ oligomer-induced synaptic and cognitive deficits
Li, Y., Chen, Y., Li, W., Huang, X., Badie-Mahdavi, H., Jian, F., Huang, T. Y., Zhao, Y., Cohen, S. N., Li, L., et al. (2016) · Scientific Reports · doi:10.1038/srep18668 · Cited by 12
Balogiannis, S. (2013) · Future Neurology · doi:10.2217/fnl.13.10 · Cited by 11
Tubulin‐Binding Region Modulates Cholesterol‐Triggered Aggregation of Tau Proteins
Ali, A., Matveyenka, M., Pickett, D. N., Rodriguez, A., & Kurouski, D. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.16294 · Cited by 10
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Sultanakhmetov, G., Kato, I., Asada, A., Saito, T., & Ando, K. (2024) · Genes to Cells · doi:10.1111/gtc.13101 · Cited by 11
“…to play a critical role in disease pathogenesis (Alonso et al., 2010; Ando, Maruko-Otake, et al., 2016; Ando, Oka, et al., 2016; Augustinack et al., 2002; Iijima et al., 2010; Iijima-Ando et al., 2012; Lasagna-Reeves et al., 2016; Nishimura et al., 2004; Yu et al., 2012; Zempel et al., 2010).”
BackgroundKIBRA repairs synaptic plasticity and promotes resilience to tauopathy-related memory loss
Kauwe, G., Pareja-Navarro, K. A., Yao, L., Chen, J. H., Wong, I., Saloner, R., Cifuentes, H., Nana, A., Shah, S., Li, Y.-Q., et al. (2023) · bioRxiv · doi:10.1101/2023.06.12.543777 · Cited by 10
“Page | 16 proteostasis (63), and cytoskeletal destabilization (64, 65).”
BackgroundTau Acts in Concert With Kinase/Phosphatase Underlying Synaptic Dysfunction
Fan, X., Xia, L., Zhou, Z., Qiu, Y., Zhao, C., Yin, X., & Qian, W. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.908881 · Cited by 14
Wischhof, L., Adhikari, A., Mondal, M., Marsal-Cots, A., Biernat, J., Mandelkow, E., Mandelkow�, E., Ehninger, D., Nicotera, P., & Bano, D. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101774 · Cited by 12
Self-citationAnti-Aβ antibodies bound to neuritic plaques enhance microglia activity and mitigate tau pathology
Laversenne, V., Nazeeruddin, S., Källstig, E., Colin, P., Voize, C., & Schneider, B. L. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01069-3 · Cited by 11
“In primary hippocampal neurons, exposure to Aβ oligomers caused tau missorting through microtubule destabilization [80], disruption of the barrier integrity of the axon initial segment [47, 70], and activation of tau acetylation [70].”
BackgroundAhmed, G. A.-R., Khalil, S., hotaby, W. E., Abbas, L., Sherif, H. H. A., Abdel‐Rahman, E. A., Saber, S. H., Hassan, M. A. E., Hassan, M. H., & Ali, S. S. (2019) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2019.117535 · Cited by 11
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Modelling neurodegenerative diseases in vitro: Recent advances in 3D iPSC technologies
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Turnbull, M. T., & Coulson, E. J. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160805 · Cited by 11
“A (cid:2) oligomers are toxic [37, 38], and can cause mis-sorting of tau into dendrites, increased tau phosphorylation, and destabilization and damage of microtubules and spines [39].”
Proteomics in Traditional Chinese Medicine with an Emphasis on Alzheimer’s Disease
Sulistio, Y. A., & Heese, K. (2015) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2015/393510 · Cited by 11
Xi, Y., Ding, J., Han, J., Zhang, D.-D., Liu, J.-M., Feng, L., & Xiao, R. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-014-0151-9 · Cited by 11
“This excessive Ca2? influx induced neuronal microtubules further fracture, mitochondrial damage, and reduction the number of synapses (Uhasz et al. 2010; Zempel et al. 2010).”
BackgroundHowells, C., Saar, K., Eaton, E. D., Ray, S., Palumaa, P., Shabala, L., Adlard, P. A., Bennett, W. R., West, A. K., Guillemin, G. J., et al. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.06.002 · Cited by 8
Synaptic scaffold protein PSD-95: a therapeutic target for Alzheimer’s disease
Fan, X., Wang, H., Ping, J., Li, M., Gu, J., & Qian, W. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.117401 · Cited by 8
Capuano, A. W., Sarsani, V., Tasaki, S., Mehta, R. I., Li, J., Ahima, R. S., Arnold, S. E., Bennett, D. A., Petyuk, V., Liang, L., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14460 · Cited by 8
Damuka, N., Irmen, R. E., Krizan, I. M., Miller, M. D., Gollapelli, K. K., Bhoopal, B., Deep, O., Bansode, A. H., Lockhart, S. N., Orr, M. E., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14083 · Cited by 9
“41 However,thereisasignificantgapinmoleculardiagnosticmechanisms capable of measuring MT dynamics and our understanding of how this relates to the primary pathologies in AD, amyloid and tau.”
Potential mechanisms underlying lithium treatment for Alzheimer's disease and COVID-19.
Wei, H.-F., Anchipolovsky, S., Vera, R., Liang, G., & Chuang, D. M. (2022) · PubMed · doi:10.26355/eurrev_202203_28369 · Cited by 8
“Although inhibition of GSK-3β and CDK-5 is thought to be one of the primary mechanisms for inducing lithium’s neuroprotective efficacies 117,118 , the role of Ca 2+ modulation in mediating lithi-um-induced neuroprotection has been under-ex-plored.”
BackgroundCuadrado‐Tejedor, M., Pérez-González, M., Alfaro‐Ruiz, R., Badesso, S., Sucunza, D., Espelosin, M., Ursúa, S., Lachén‐Montes, M., Fernández‐Irigoyen, J., Santamaría, E., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111950 · Cited by 11
“The presence of tau in the dendrites may represent an early event preceding dendritic spines loss, local increase in Ca2+, microtubule destabilization and mitochondria depletion [25].”
BackgroundBell, M., Bachmann, S., Klimek, J., Langerscheidt, F., & Zempel, H. (2020) · bioRxiv · doi:10.1101/2020.06.26.173526 · Cited by 9
Self-citationKneynsberg, A., & Kanaan, N. M. (2017) · eNeuro · doi:10.1523/eneuro.0043-17.2017 · Cited by 11
“This information is important considering the contention in the field that tau mislocalization is important in AD and the recent focus on the role of the AIS in tau distribution (Zempel et al., 2010; Li et al., 2011; Sohn et al., 2016).”
BackgroundThe Microtubule-Associated Protein 1A (MAP1A) is an Early Molecular Target of Soluble Aβ-Peptide
Clemmensen, C., Aznar, S., Knudsen, G. M., & Klein, A. B. (2012) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-011-9796-9 · Cited by 9
“A recent study showed that the earliest microscopy-visible effect of oligomeric Ab was a disturbed sorting of tau protein into dendritic compartments, immediately resulting in dendritic spine retraction and loss of synaptic protein markers (Zempel et al. 2010).”
BackgroundBraak, H., & Tredici, K. D. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_22 · Cited by 11
Mechanisms of Neuronal Microtubule Loss in Alzheimer’s Disease
Austin, T. O., Liang, Q., & Baas, P. W. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803690-7.00004-1 · Cited by 9
Lari, M. Q., Kumar, A., Ashesh, A. M., Kumar, D., Singh, B., & Kumar, D. (2025) · Current Neuropharmacology · doi:10.2174/011570159x379926250801062557 · Cited by 7
“Nevertheless, peptides raise intraneuronal calcium concentrations, which in turn trigger calpain activation, cleave p35 to p25, and ultimately lead to dysregulation of CDK5 activity [48].”
Oh, Y. R., & Shin, M. (2025) · BMB Reports · doi:10.5483/bmbrep.2025-0077 · Cited by 9
“Several factors — including exposure to A — have been shown to promote this aberrant mislocalization (79-81), with tau acetylation emerging as one of the driving mechanisms (46, 77, 82).”
García-Carlos, C. A., Basurto‐Islas, G., Perry, G. L., & Mondragón‐Rodríguez, S. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-231365 · Cited by 9
Robles-Gómez, Á. A., Ordaz, B., Lorea-Hernández, J. J., & Peña‐Ortega, F. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1198299 · Cited by 8
Venkataraman, L., He, P., Schulz, P., & Sierks, M. R. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.04.014 · Cited by 9
Transcriptome Profile of Nicotinic Receptor-Linked Sensitization of Beta Amyloid Neurotoxicity
Arora, K., Belcaid, M., Lantz, M. J., Taketa, R., & Nichols, R. A. (2020) · Scientific Reports · doi:10.1038/s41598-020-62726-0 · Cited by 10
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Small, D. (2012) · Neurodegenerative Diseases · doi:10.1159/000333126 · Cited by 8
Overview and recent advances in neuropathology. Part 2: Neurodegeneration
Masters, C. L., Kril, J. J., Halliday, G. M., Pamphlett, R., Collins, S. J., Hill, A. F., & McLean, C. (2011) · Pathology · doi:10.1097/pat.0b013e3283426eee · Cited by 13
“This in turn invokes a pathway which involves fyn (a kinase) and calcineurin (a phosphatase) ultimately leading to the accumulation of the tau MAP.6,7 It remains to be determined how these phosphorylation/dephosphorylation events might play into the cascade that leads to Unauthorized reproduction of this article is pr…”
BackgroundRelationship Between Tau, β Amyloid and α-Synuclein Pathologies
Walker, L., & Attems, J. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_14 · Cited by 12
Zempel, H. (2023) · Cytoskeleton · doi:10.1002/cm.21793 · Cited by 7
“We pinpointed TAU missorting as a very early event in the disease progression in experiments with cultured neurons (Bell et al., 2021; Zempel et al., 2010; Zempel & Mandelkow, 2014), in agreement with appearance of non-aggregated TAU in the soma and dendrites in AD (Braak et al., 1994; Braak et…”
BackgroundSelf-citationSteele-Nicholson, L. J., & Andrews, M. R. (2022) · Cells · doi:10.3390/cells11060937 · Cited by 7
“of axonal proteins may cause or contribute to neuropathology, such as in Alzheimer’s disease and amyotrophic lateral sclerosis [3,4].”
BackgroundGnanaprakash, M., Staniszewski, A., Zhang, H., Pitstick, R., Kavanaugh, M. P., Arancio, O., & Nicholls, R. E. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-200462 · Cited by 9
Aβ oligomer induced cognitive impairment and evaluation of ACU193‐MNS‐based MRI in rabbit
Rozema, N. B., Procissi, D., Bertolino, N., Viola, K. L., Nandwana, V., Abdul, N., Pribus, S. J., Dravid, V. P., Klein, W. L., Disterhoft, J. F., et al. (2020) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.12087 · Cited by 6
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JNK-interacting protein 1 mediates Alzheimer's-like pathological features in AICD-transgenic mice
Margevicius, D., Bastian, C., Fan, Q., Davis, R. J., & Pimplikar, S. W. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.04.013 · Cited by 7
“Abbreviations: AICD dehydrogenase; JIP1, c-Jun N-terminal kinaseeinteracting protein 1; Tg, transgenic. aggregation that mediates loss of dendritic spines (Chabrier et al., 2014; Kopeikina et al., 2013a, 2013b; Zempel et al., 2010).”
BackgroundDerailed Intraneuronal Signalling Drives Pathogenesis in Sporadic and Familial Alzheimer’s Disease
Dooren, T. V., Princen, K., Witte, K. D., & Griffioen, G. (2014) · BioMed Research International · doi:10.1155/2014/167024 · Cited by 9
“Collectively, it seems possible that deregulation of signalling by hyperphosphorylated TAU constitutes a toxic gain-of-function of TAU driving pathogenesis in AD (Figure 1).”
BackgroundNeurodegeneration in familal amyloidotic polyneuropathy
Gasperini, R., & Small, D. H. (2011) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2011.05607.x · Cited by 8
“doses, such as Alzheimer’s disease, where accumulation and deposition of amyloid-beta protein has been associated with disrupted calcium homeostasis in neurons.(32,62,63)”
BackgroundPotential Therapeutic Strategies to Prevent the Progression of Alzheimer to Disease States
Aso, E., & Ferrer, I. (2013) · InTech eBooks · doi:10.5772/54783 · Cited by 5
“The anti-mitotic drug paclitaxel prevents Aβ-induced toxicity in cell culture [89], as well as axonal transport deficits and behavioral impairments in tau transgenic mice [90].”
IgLON5 autoimmune antibodies activate Tau via neuronal hyperactivity
Askin, B., Kilic, C., Gómez, C. C., Duong, S. L.-L., Dominguez‐Baquero, A., Goihl, A., Nalbach, K., Petushi, J., Grundschöttel, P., Wagner, J., et al. (2026) · Science Advances · doi:10.1126/sciadv.aec2042 · Cited by 9
“Anti-IgLON5 disease patients, whose α - IgLON5 ABB and pCtrl AB pools were isolated in this study, were patients in the neurology clinics of the Charité University Medicine Berlin (patients: IgLON5#2,3,4) and of the Otto- von- Guericke-University Magdeburg (patient: IgLON5#1) (Table 1).”
Neupane, S., & Hortobágyi, T. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262411811 · Cited by 6
“…research by Zempel and colleagues showed that A β oligomers acutely drive somatodendritic mis-Int sorting of tau, accompanied by local dendritic spine loss and increased tau phosphorylation via Ca 2+ /CDK5-dependent pathways, thereby priming tau aggregation in primary rat hippocampal neurons [124].”
Shang, H., Duan, M., Da, C., Fu, X., & Zhang, T. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.144651 · Cited by 5
Fourrière, L., & Gleeson, P. A. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1550211 · Cited by 6
Bell-Simons, M., Buchholz, S., Klimek, J., & Zempel, H. (2023) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-023-01359-z · Cited by 8
Self-citationHuang, Z. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221042 · Cited by 12
Challenges in understanding the structure/activity relationship of Aβ oligomers
Pilkington, A. W., & Legleiter, J. A. (2019) · AIMS Biophysics · doi:10.3934/biophy.2019.1.1 · Cited by 7
Amyloid Plaques Show Binding Capacity of Exogenous Injected Amyloid-β
Gureviciene, I., Gurevicius, K., Mugantseva, E., Kislin, M., Khiroug, L. S., & Tanila, H. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160453 · Cited by 8
Simulated Cytoskeletal Collapse via Tau Degradation
Sendek, A. D., Fuller, H. R., Hayre, N. R., Singh, R., & Cox, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0104965 · Cited by 6
Metadata
- Authors
- Zempel, H., Thies, E., Mandelkow, E., & Mandelkow, E.-M.
- Affiliations
- Max Planck Unit for Structural Molecular Biology (DE)
- German Center for Neurodegenerative Diseases (DE)
- Corresponding author
- Mandelkow, Eva-Maria
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2010-09-08
- Volume
- 30
- Issue
- 36
- Pages
- 11938-11950
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6633549
- OpenAlex
- W2041956586
- Cited by
- 686
- References
- 70
- Citations by year
- 2026: 29 · 2025: 33 · 2024: 27 · 2023: 22 · 2022: 30 · 2021: 38 · 2020: 54 · 2019: 46 · 2018: 49 · 2017: 46 · 2016: 50 · 2015: 51 · 2014: 61 · 2013: 54 · 2012: 50
- FWCI
- 32.49
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- DZNE Pub (submittedVersion)
- Funders
- European Commission
- Deutsche Forschungsgemeinschaft
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta oligomers, Alzheimer's disease, tau phosphorylation, dendrites, microtubule destabilization, dendritic spines, neurofilaments, mitochondria, paclitaxel, p70S6K, cyclin-dependent kinase 5, hippocampal neurons, axonal transport, oxidative stress, glutamate, serum deprivation
- MeSH terms
- Adenosine Triphosphate, Analysis of Variance, Animals, Calcium, Cells, Cultured, Dendrites, Embryo, Mammalian, Hippocampus, L-Lactate Dehydrogenase, Microtubules, Mitochondria, Neurons, Peptide Fragments, Phosphorylation, Protein Kinases, Time Factors, Amyloid beta-Peptides, tau Proteins, Neurofilament Proteins, Rats, Sprague-Dawley, Protein Transport, Microscopy, Electron, Transmission, Dendritic Spines, Rats
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