The many faces of tau

Morris, Meaghan; Maeda, Sumihiro; Vossel, Keith; Mucke, Lennart

doi:10.1016/j.neuron.2011.04.009

Cited by 900Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsMicrotubule and mitosis dynamics

The many faces of tau

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Morris, Meaghan, Maeda, Sumihiro, Vossel, Keith, Mucke, Lennart·2011·Neuron

DOI 10.1016/j.neuron.2011.04.009PMC PMC3319390

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Abstract

While the microtubule-binding capacity of the protein tau has been known for many years, new functions of tau in signaling and cytoskeletal organization have recently emerged. In this review, we highlight these functions and the potential roles of tau in neurodegenerative disease. We also discuss the therapeutic potential of drugs targeting various aspects of tau biology.

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In mice, a 50% reduction of endogenous tau markedly reduces amyloid β- and ApoE4 fragment-induced neuronal and cognitive impairments in vivo.
“markedly reduces amyloid 𝛃 and ApoE4 fragment-induced neuronal and cognitive impairments in vivo (34)”
From An Unbiased Approach to Identifying Tau Kinases That Phosphorylate Tau at Sites Associated with Alzheimer Disease (2013) · cites this paper as [34]
The section “Reduction of overall tau levels” says that partial tau reduction in mice markedly diminishes Aβ- and ApoE-induced neuronal and cognitive impairments in vivo. The copy does not specify a 50% reduction for this result or identify the ApoE-induced impairments as caused by ApoE4 fragments; “Tau Functions Enabling Pathogenesis” discusses apoE4 more generally. Page numbers were not available in the indexed passages. (LLM, conf=0.85)
Experimental — accuracy not yet measured
Reductions in tau levels prevent amyloid β from causing neuronal deficits in cell culture and in transgenic mice expressing human amyloid precursor protein.
“Reductions in tau levels have also been shown to prevent amyloid 𝛃 from causing neuronal deficits in cell culture and in transgenic mice expressing human amyloid precursor protein (34).”
From An Unbiased Approach to Identifying Tau Kinases That Phosphorylate Tau at Sites Associated with Alzheimer Disease (2013) · cites this paper as [34]
In mice, a 50% reduction of endogenous tau is well tolerated.
“in mice a 50% reduction of endogenous tau is well tolerated”
From An Unbiased Approach to Identifying Tau Kinases That Phosphorylate Tau at Sites Associated with Alzheimer Disease (2013) · cites this paper as [34]
The 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.”
From Tau co-organizes dynamic microtubule and actin networks (2015) · cites this paper as [34]
Tauopathies are neurodegenerative diseases characterized by pathological accumulation of hyper-phosphorylated tau in paired helical filaments or neurofibrillary tangles within neurons and glia of affected brain regions, leading to cell death.
“Tauopathies are neurodegenerative diseases characterized by aberrant forms of tau protein accumulation leading to neuronal death in focal brain areas.”
From Targeted degradation of aberrant tau in frontotemporal dementia patient-derived neuronal cell models (2019) · cites this paper as Morris et al., 2011

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Neuron-Specific Apolipoprotein E4 Proteolysis Is Associated with Increased Tau Phosphorylation in Brains of Transgenic Mice
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Small Ubiquitin-like Modifier (SUMO) Modification of Natively Unfolded Proteins Tau and α-Synuclein
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Alzheimer Disease-specific Conformation of Hyperphosphorylated Paired Helical Filament-Tau Is Polyubiquitinated through Lys-48, Lys-11, and Lys-6 Ubiquitin Conjugation
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Granular Tau Oligomers as Intermediates of Tau Filaments
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Update on the biomarker core of the Alzheimer's Disease Neuroimaging Initiative subjects
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Tau-induced defects in synaptic plasticity, learning, and memory are reversible in transgenic mice after switching off the toxic Tau mutant
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Trehalose ameliorates dopaminergic and tau pathology in parkin deleted/tau overexpressing mice through autophagy activation
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The Potential for β-Structure in the Repeat Domain of Tau Protein Determines Aggregation, Synaptic Decay, Neuronal Loss, and Coassembly with Endogenous Tau in Inducible Mouse Models of Tauopathy
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Proline-directed Pseudo-phosphorylation at AT8 and PHF1 Epitopes Induces a Compaction of the Paperclip Folding of Tau and Generates a Pathological (MC-1) Conformation
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A Spatial Gradient of Tau Protein Phosphorylation in Nascent Axons
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Changed Conformation of Mutant Tau-P301L Underlies the Moribund Tauopathy, Absent in Progressive, Nonlethal Axonopathy of Tau-4R/2N Transgenic Mice
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The Generation of a 17 kDa Neurotoxic Fragment: An Alternative Mechanism by which Tau Mediates β-Amyloid-Induced Neurodegeneration
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Process Outgrowth of Oligodendrocytes Is Promoted by Interaction of Fyn Kinase with the Cytoskeletal Protein Tau
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Tau Binds to the Distal Axon Early in Development of Polarity in a Microtubule- and Microfilament-Dependent Manner
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Anionic Micelles and Vesicles Induce Tau Fibrillization in Vitro
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Extracellular tau is toxic to neuronal cells
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Tubulin requires tau for growth onto microtubule initiating sites.
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Insulin Dysfunction InducesIn VivoTau Hyperphosphorylation through Distinct Mechanisms
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Tau Protects Microtubules in the Axon from Severing by Katanin
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Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells
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Inhibition of tau phosphorylating protein kinase cdk5 prevents β‐amyloid‐induced neuronal death
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Phosphorylation Regulates Tau Interactions with Src Homology 3 Domains of Phosphatidylinositol 3-Kinase, Phospholipase Cγ1, Grb2, and Src Family Kinases
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Interaction of Tau with the Neural Membrane Cortex Is Regulated by Phosphorylation at Sites That Are Modified in Paired Helical Filaments
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CSF biomarkers predict a more malignant outcome in Alzheimer disease
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Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice
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Activity-Dependent Neuroprotective Protein Snippet NAP Reduces Tau Hyperphosphorylation and Enhances Learning in a Novel Transgenic Mouse Model
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“The peptide NAP stabilizes microtubules (Divinski et al., 2006) and reduces tau hyperphosphorylation (Vulih-Shultzman et al., 2007), suggesting that microtubule-stabilizing compounds can have more than one mechanism of action.”
Background
Disease-related Modifications in Tau Affect the Interaction between Fyn and Tau
Bhaskar, K., Yen, S.-H. C., & Lee, G. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505895200 · Cited by 219 · see citing works
Tau-dependent microtubule disassembly initiated by prefibrillar β-amyloid
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Parkinsonism, Lrrk2 G2019S, and tau neuropathology
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Lithium: Updated Human Knowledge Using an Evidence-Based Approach
Grandjean, E. M., & Aubry, J. (2009) · CNS Drugs · doi:10.2165/00023210-200923040-00005 · Cited by 208 · see citing works
In vivo evidence of CHIP up‐regulation attenuating tau aggregation
Sahara, N., Murayama, M., Mizoroki, T., Urushitani, M., Imai, Y., Takahashi, R., Murata, S., Tanaka, K., & Takashima, A. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03272.x · Cited by 208 · see citing works
Lithium: Updated Human Knowledge Using an Evidence-Based Approach
Grandjean, E. M., & Aubry, J. (2009) · CNS Drugs · doi:10.2165/00023210-200923050-00004 · Cited by 208 · see citing works
τ Is Widely Expressed in Rat Tissues
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Assembly of two distinct dimers and higher‐order oligomers from full‐length tau
Sahara, N., Maeda, S., Murayama, M., Suzuki, T., Dohmae, N., Yen, S.-H. C., & Takashima, A. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05555.x · Cited by 192 · see citing works
Self-citation
A Cdk5 inhibitory peptide reduces tau hyperphosphorylation and apoptosis in neurons
Zheng, Y., Kesavapany, S., Gravell, M., Hamilton, R. S., Schubert, M., Amin, N. D., Albers, W., Grant, P. G., & Pant, H. C. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600441 · Cited by 190 · see citing works
Axonal Transport RatesIn VivoAre Unaffected by Tau Deletion or Overexpression in Mice
Yuan, A., Kumar, A. R., Peterhoff, C. M., Duff, K., & Nixon, R. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.5242-07.2008 · Cited by 187 · see citing works
Structural and functional changes in tau mutant mice neurons are not linked to the presence of NFTs
Rocher, A. B., Crimins, J. L., Amatrudo, J. M., Kinson, M. S., Todd-Brown, M. A., Lewis, J., & Luebke, J. I. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2009.07.029 · Cited by 187 · see citing works
Tau Phosphorylation Sites Work in Concert to Promote Neurotoxicity In Vivo
Steinhilb, M. L., Dias-Santagata, D., Fulga, T. A., Felch, D. L., & Feany, M. B. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-04-0327 · Cited by 187 · see citing works
Tau – an inhibitor of deacetylase HDAC6 function
Perez, M., Santa‐Maria, I., De Barreda, E. G., Zhu, X., Cuadros, R., Cabrero, J. R., Sanchez‐Madrid, F., Dawson, H. N., Vitek, M. P., Perry, G., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06102.x · Cited by 182 · see citing works
Developmental regulation of tau phosphorylation, tau kinases, and tau phosphatases
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Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden
O’Leary, J. C., Li, Q., Marinec, P. S., Blair, L. J., Congdon, E. E., Johnson, A. G., Jinwal, U. K., Koren, J., Jones, J. R., Kraft, C., et al. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-45 · Cited by 176 · see citing works
Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice
Boimel, M., Grigoriadis, N., Lourbopoulos, A., Haber, E., Abramsky, O., & Rosenmann, H. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2010.05.010 · Cited by 174 · see citing works
Activation of Phospholipase C-γ by the Concerted Action of Tau Proteins and Arachidonic Acid
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Paired helical filament tau (PHFtau) in Niemann-Pick type C disease is similar to PHFtau in Alzheimer's disease
Auer, I., Schmidt, M., Lee, V., Curry, B., Suzuki, K., Shin, R., Pentchev, P., Carstea, E., & Trojanowski, J. (2004) · Acta Neuropathologica · doi:10.1007/bf00318566 · Cited by 169 · see citing works
The Role of Tau Phosphorylation in the Pathogenesis of Alzheimers Disease
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Fyn Kinase Modulates Synaptotoxicity, But Not Aberrant Sprouting, in Human Amyloid Precursor Protein Transgenic Mice
Chin, J., Palop, J. J., Yu, G.-Q., Kojima, N., Masliah, E., & Mucke, L. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0277-04.2004 · Cited by 161 · see citing works
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Conformational changes specific for pseudophosphorylation at serine 262 selectively impair binding of tau to microtubules
Fischer, D., Mukrasch, M. D., Biernat, J., Bibow, S., Blackledge, M., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2009) · Biochemistry · doi:10.1021/bi901090m · Cited by 149 · see citing works
Selective Destruction of Stable Microtubules and Axons by Inhibitors of Protein Serine/Threonine Phosphatases in Cultured Human Neurons (NT2N Cells)
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Structure, Microtubule Interactions, and Phosphorylation of Tau Proteina
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The proline-rich domain of tau plays a role in interactions with actin
He, H. J., Wang, X. S., Pan, R., Wang, D. L., Liu, M. N., & He, R. Q. (2009) · BMC Cell Biology · doi:10.1186/1471-2121-10-81 · Cited by 142 · see citing works
Surface-decoration of Microtubules by Human Tau
Santarella, R. A., Skiniotis, G., Goldie, K. N., Tittmann, P., Gross, H., Mandelkow, E., Mandelkow, E., & Hoenger, A. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.04.008 · Cited by 141 · see citing works
A role for FKBP52 in tau protein function
Chambraud, B., Sardin, E., Giustiniani, J., Dounane, O., Schumacher, M., Goedert, M., & Baulieu, E.-E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914957107 · Cited by 140 · see citing works
Loss of tau elicits axonal degeneration in a mouse model of Alzheimer's disease
Dawson, H. N., Cantillana, V., Jansen, M., Wang, H., Vitek, M. P., Wilcock, D. M., Lynch, J., & Laskowitz, D. T. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.04.037 · Cited by 137 · see citing works
GSK-3β Is Required for Memory Reconsolidation in Adult Brain
Kimura, T., Yamashita, S., Nakao, S., Park, J.-M., Murayama, M., Mizoroki, T., Yoshiike, Y., Sahara, N., & Takashima, A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003540 · Cited by 136 · see citing works
Axonal Degeneration Induced by Targeted Expression of Mutant Human Tau in Oligodendrocytes of Transgenic Mice That Model Glial Tauopathies
Higuchi, M., Zhang, B., Forman, M. S., Yoshiyama, Y., Trojanowski, J. Q., & Lee, V. M. ‐. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.2691-05.2005 · Cited by 127 · see citing works
U‐box protein carboxyl terminus of Hsc70‐interacting protein (CHIP) mediates poly‐ubiquitylation preferentially on four‐repeat Tau and is involved in neurodegeneration of tauopathy
Hatakeyama, S., Matsumoto, M., Kamura, T., Murayama, M., Chui, D.-H., Planel, E., Takahashi, R., Nakayama, K. I., & Takashima, A. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02713.x · Cited by 127 · see citing works
Divergent Pathways Mediate Spine Alterations and Cell Death Induced by Amyloid-β, Wild-Type Tau, and R406W Tau
Tackenberg, C., & Brandt, R. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.3590-09.2009 · Cited by 127 · see citing works
Hope in Alzheimer's fight emerges from unexpected places
Gura, T. (2008) · Nature Medicine · doi:10.1038/nm0908-894 · Cited by 123 · see citing works
Immunotherapy Targeting Pathological Tau Protein in Alzheimer's Disease and Related Tauopathies
Sigurdsson, E. M. (2008) · Journal of Alzheimer's Disease · doi:10.3233/jad-2008-15202 · Cited by 116 · see citing works
Progressive neurodegeneration in C. elegans model of tauopathy
Miyasaka, T., Ding, Z., Gengyo-Ando, K., Oue, M., Yamaguchi, H., Mitani, S., & Ihara, Y. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.03.017 · Cited by 115 · cited 1× · see citing works
“In sensory neurons of C. elegans, overexpression of 4R0N tau decreased the response to touch, and this phenotype was exacerbated by heat shock when tested after a recovery period of 24 hr (Miyasaka et al., 2005a).”
Background
Somatodendritic localization of phosphorylated tau in neonatal and adult rat cerebral cortex
Tashiro, K., Hasegawa, M., Ihara, Y., & Iwatsubo, T. (1997) · Neuroreport · doi:10.1097/00001756-199708180-00029 · Cited by 109 · see citing works
The pathogenesis of Niemann–Pick type C disease: a role for autophagy?
Pacheco, C. D., & Lieberman, A. P. (2008) · Expert Reviews in Molecular Medicine · doi:10.1017/s146239940800080x · Cited by 109 · see citing works
Peptide neuroprotection through specific interaction with brain tubulin
Divinski, I., Holtser‐Cochav, M., Vulih, I., Steingart, R. A., & Gozes, I. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03936.x · Cited by 108 · see citing works
Cleavage of Tau by calpain in Alzheimer's disease: the quest for the toxic 17 kD fragment
Garg, S., Timm, T., Mandelkow, E.-M., Mandelkow, E., & Wang, Y. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.09.008 · Cited by 103 · see citing works
High throughput screening for small molecule inhibitors of heparin-induced tau fibril formation
Crowe, A., Ballatore, C., Hyde, E. G., Trojanowski, J. Q., & Lee, V. M. ‐. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.03.056 · Cited by 101 · see citing works
Essential role of tau phosphorylation in adult hippocampal neurogenesis
Hong, X., Peng, C., Wei, W., Tian, Q., Liu, Y., Yao, X., Zhang, Y., Cao, F., Wang, Q., & Wang, J. (2009) · Hippocampus · doi:10.1002/hipo.20712 · Cited by 99 · see citing works
Tau oligomerization: a role for tau aggregation intermediates linked to neurodegeneration
Sahara, N., Maeda, S., & Takashima, A. (2008) · Current Alzheimer Research · doi:10.2174/156720508786898442 · Cited by 99 · see citing works
Self-citation
Aggregation of Detergent-insoluble Tau Is Involved in Neuronal Loss but Not in Synaptic Loss
Kimura, T., Fukuda, T., Sahara, N., Yamashita, S., Murayama, M., Mizoroki, T., Yoshiike, Y., Lee, B., Sotiropoulos, I., Maeda, S., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.136630 · Cited by 97 · see citing works
Self-citation
Calmodulin inhibits interaction of actin with MAP2 and Tau, two major microtubule-associated proteins.
Kotani, S., Nishida, E., Kumagai, H., & Sakai, H. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85149-9 · Cited by 93 · see citing works
Transglutaminases and Transglutaminase‐Catalyzed Cross‐Links Colocalize with the Pathological Lesions in Alzheimer's Disease Brain
Wilhelmus, M. M. M., Grunberg, S. C. S., Bol, J. G. J. M., van Dam, A., Hoozemans, J. J. M., Rozemüller, A. J. M., & Drukarch, B. (2008) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00197.x · Cited by 90 · see citing works
Molecular chaperone‐mediated tau protein metabolism counteracts the formation of granular tau oligomers in human brain
Sahara, N., Maeda, S., Yoshiike, Y., Mizoroki, T., Yamashita, S., Murayama, M., Park, J. ‐., Saito, Y., Murayama, S., & Takashima, A. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21417 · Cited by 89 · see citing works
Self-citation
Addressing Alzheimers Disease Tangles: From NAP to AL-108
Gozes, I., Stewart, A. J., Morimoto, B. H., Fox, A. W., Sutherland, K., & Schmechel, D. E. (2009) · Current Alzheimer Research · doi:10.2174/156720509789207895 · Cited by 89 · see citing works
Tau-Focused Immunotherapy for Alzheimers Disease and Related Tauopathies
Sigurdsson, E. M. (2009) · Current Alzheimer Research · doi:10.2174/156720509789207930 · Cited by 87 · see citing works
The structure of divalent cation-induced aggregates of PIP2 and their alteration by gelsolin and tau
Flanagan, L. A., Cunningham, C. C., Chen, J., Prestwich, G. D., Kosik, K. S., & Janmey, P. A. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78176-1 · Cited by 87 · see citing works
Differential Binding of Apolipoprotein E Isoforms to Tau and Other Cytoskeletal Proteins
Fleming, L. M., Weisgraber, K. H., Strittmatter, W. J., Troncoso, J. C., & Johnson, G. V. W. (1996) · Experimental Neurology · doi:10.1006/exnr.1996.0064 · Cited by 82 · see citing works
Drosophila models of human tauopathies indicate that Tau protein toxicity in vivo is mediated by soluble cytosolic phosphorylated forms of the protein
Feuillette, S., Miguel, L., Frébourg, T., Campion, D., & Lecourtois, M. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06663.x · Cited by 81 · see citing works
Tangle-Bearing Neurons Survive Despite Disruption of Membrane Integrity in a Mouse Model of Tauopathy
de Calignon, A., Spires-Jones, T. L., Pitstick, R., Carlson, G. A., & Hyman, B. T. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181a9fc66 · Cited by 81 · see citing works
A possible link between astrocyte activation and tau nitration in Alzheimer's disease
Reyes, J. F., Reynolds, M. R., Horowitz, P. M., Fu, Y., Guillozet-Bongaarts, A. L., Berry, R., & Binder, L. I. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.04.005 · Cited by 80 · see citing works
Tau complexes with phospholipase C-γ in situ
Jenkins, S. M., & Johnson, G. V. W. (1998) · Neuroreport · doi:10.1097/00001756-199801050-00014 · Cited by 78 · see citing works
Secretion of human tau fragments resembling CSF‐tau in Alzheimer's disease is modulated by the presence of the exon 2 insert
Kim, W., Lee, S., & Hall, G. F. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.05.042 · Cited by 78 · see citing works
Changes in microtubule turnover accompany synaptic plasticity and memory formation in response to contextual fear conditioning in mice
Fanara, P., Husted, K. H., Selle, K., Wong, P. A., Banerjee, J., Brandt, R., & Hellerstein, M. K. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.03.031 · Cited by 77 · see citing works
Splicing of a Regulated Exon Reveals Additional Complexity in the Axonal Microtubule‐Associated Protein Tau
Wei, M., & Andreadis, A. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70041346.x · Cited by 75 · see citing works
Tau impacts on growth-factor-stimulated actin remodeling
Sharma, V. M., Litersky, J. M., Bhaskar, K., & Lee, G. S. (2007) · Journal of Cell Science · doi:10.1242/jcs.03378 · Cited by 75 · see citing works
Tyrosine phosphorylation of tau accompanies disease progression in transgenic mouse models of tauopathy
Bhaskar, K., Hobbs, G. A., Yen, S.-H., & Lee, G. S. (2010) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2010.01103.x · Cited by 74 · see citing works
Tau deletion exacerbates the phenotype of Niemann–Pick type C mice and implicates autophagy in pathogenesis
Pacheco, C. D., Elrick, M. J., & Lieberman, A. P. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn423 · Cited by 74 · see citing works
LRRK2 and neurodegeneration
Santpere, G., & Ferrer, I. (2009) · Acta Neuropathologica · doi:10.1007/s00401-008-0478-8 · Cited by 73 · see citing works
Tau associates with actin in differentiating PC12 cells
Yu, J.-Z., & Rasenick, M. M. (2006) · The FASEB Journal · doi:10.1096/fj.05-5206com · Cited by 72 · see citing works
Niemann-Pick disease type C yields possible clue for why cerebellar neurons do not form neurofibrillary tangles.
Bu, B.-T., Klunemann, H., Suzuki, K., Li, J., Bird, T., Jin, L.-W., & Vincent, I. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0551 · Cited by 63 · see citing works
Microtubule‐associated protein tau in human prostate cancer cells: Isoforms, phosphorylation, and interactions
Souter, S., & Lee, G. S. (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22287 · Cited by 62 · see citing works
Expression of embryonic tau protein isoforms persist during adult neurogenesis in the hippocampus
Bullmann, T., de Silva, R., Holzer, M., Mori, H., & Arendt, T. (2006) · Hippocampus · doi:10.1002/hipo.20255 · Cited by 62 · see citing works
Lysosomal Protease Inhibitors Induce Meganeurites and Tangle-like Structures in Entorhinohippocampal Regions Vulnerable to Alzheimer's Disease
Bi, X., Zhou, J., & LYNCH, G. S. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7087 · Cited by 57 · see citing works
Monte Carlo Simulations of Tau Proteins: Effect of Phosphorylation
Jho, Y., Zhulina, E. B., Kim, M. W., & Pincus, P. A. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.06.056 · Cited by 55 · see citing works
Tubulin, actin, and tau protein interactions and the study of their macromolecular assemblies
Farias, G. A., Muñoz, J. P., Garrido, J., & Maccioni, R. B. (2002) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10133 · Cited by 54 · see citing works
τ Regulation of Microtubule‐Microtubule Spacing and Bundling
Frappier, T. F., Georgieff, I. S., Brown, K., & Shelanski, M. L. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63062288.x · Cited by 53 · see citing works
Tau Potentiates Nerve Growth Factor-induced Mitogen-activated Protein Kinase Signaling and Neurite Initiation without a Requirement for Microtubule Binding
Leugers, C. J., & Lee, G. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.105387 · Cited by 51 · see citing works
Alterations in Tau Phosphorylation in Rat and Human Neocortical Brain Slices Following Hypoxia and Glucose Deprivation
Burkhart, K., Beard, D. C., Lehman, R. A. W., & Billingsley, M. L. (1998) · Experimental Neurology · doi:10.1006/exnr.1998.6899 · Cited by 46 · see citing works
Amyloid β protein deposition in patients with frontotemporal lobar degeneration: relationship to age and apolipoprotein E genotype
Mann, D. M. A., McDonagh, A. M., Pickering-Brown, S. M., Kowa, H., & Iwatsubo, T. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)01785-2 · Cited by 41 · see citing works
Visualization of Newly Deposited tau in Neurofibrillary Tangles and Neuropil Threads
Miyasaka, T., Watanabe, A., Saito, Y., Murayama, S., Mann, D. M. A., Yamazaki, M., Ravid, R., Morishima‐Kawashima, M., Nagashima, K., & Ihara, Y. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000173890.79058.1d · Cited by 40 · see citing works
The Difference in the Binding of Phosphatidylinositol Distinguishes MAP2 from MAP2C and Tau
Surridge, C. D., & Burns, R. G. (1994) · Biochemistry · doi:10.1021/bi00192a009 · Cited by 39 · see citing works
Role of tau protein on neocortical and hippocampal oscillatory patterns
Cantero, J. L., Moreno‐López, B., Portillo, F., Rubio, A., Hita-Yáñez, E., & Ávila, J. (2010) · Hippocampus · doi:10.1002/hipo.20798 · Cited by 32 · see citing works
PHF and PHF-like fibrils –cause or consequence?
Ihara, Y. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00200-1 · Cited by 28 · see citing works
Neuron-specific recombination by Cre recombinase inserted into the murine tau locus
Muramatsu, K., Hashimoto, Y., Uemura, T., Kunii, M., Harada, R., Sato, T., Morikawa, A., & Harada, A. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.03.103 · Cited by 26 · see citing works
Deletion of tau attenuates heat shock‐induced injury in cultured cortical neurons
Miao, Y., Chen, J., Zhang, Q., & Sun, A. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22188 · Cited by 19 · see citing works

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Alzheimer Mechanisms and Therapeutic Strategies
Huang, Y., & Mucke, L. (2012) · Cell · doi:10.1016/j.cell.2012.02.040 · Cited by 1,758 · see citing works
Self-citation
Mechanisms of stress in the brain
McEwen, B. S., Bowles, N. P., Gray, J. D., Hill, M. N., Hunter, R. G., Karatsoreos, I. N., & Nasca, C. (2015) · Nature Neuroscience · doi:10.1038/nn.4086 · Cited by 1,386 · see citing works
Impairment of Glymphatic Pathway Function Promotes Tau Pathology after Traumatic Brain Injury
Iliff, J. J., Chen, M. J., Plog, B. A., Zeppenfeld, D. M., Soltero, M., Yang, L., Singh, I., Deane, R., & Nedergaard, M. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3020-14.2014 · Cited by 1,159 · see citing works
Network abnormalities and interneuron dysfunction in Alzheimer disease
Palop, J. J., & Mucke, L. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.141 · Cited by 1,022 · see citing works
Self-citation
Roles of tau protein in health and disease
Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003 · see citing works
Neurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000 · see citing works
Self-citation
Biochemistry and Cell Biology of Tau Protein in Neurofibrillary DegenerationPreprint
Mandelkow, E., & Mandelkow, E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006247 · Cited by 839 · see citing works
Tau Protein Hyperphosphorylation and Aggregation in Alzheimer’s Disease and Other Tauopathies, and Possible Neuroprotective Strategies
Šimić, G., Leko, M. B., Wray, S., Harrington, C. R., Delalle, I., Milošević, N. J., Bažadona, D., Buée, L., de Silva, R., Giovanni, G. D., et al. (2016) · Biomolecules · doi:10.3390/biom6010006 · Cited by 698 · see citing works
Tau and tauopathies
Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609 · see citing works
Aβ induces astrocytic glutamate release, extrasynaptic NMDA receptor activation, and synaptic loss
Talantova, M., Sanz-Blasco, S., Zhang, X., Xia, P., Akhtar, M. W., Okamoto, S.-I., Dziewczapolski, G., Nakamura, T., Cao, G., Pratt, A. E., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306832110 · Cited by 600 · see citing works
Reactive microglia drive tau pathology and contribute to the spreading of pathological tau in the brain
Maphis, N., Xu, G., Kokiko-Cochran, O. N., Jiang, S., Cardona, A., Ransohoff, R. M., Lamb, B. T., & Bhaskar, K. (2015) · Brain · doi:10.1093/brain/awv081 · Cited by 595 · see citing works
Physiologic brain activity causes DNA double-strand breaks in neurons, with exacerbation by amyloid-β
Suberbielle, E., Sanchez, P. E., Kravitz, A. V., Wang, X., Ho, K., Eilertson, K., Devidze, N., Kreitzer, A. C., & Mucke, L. (2013) · Nature Neuroscience · doi:10.1038/nn.3356 · Cited by 487 · see citing works
Self-citation
Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice
Morris, M., Knudsen, G. M., Maeda, S., Trinidad, J. C., Ioanoviciu, A., Burlingame, A. L., & Mucke, L. (2015) · Nature Neuroscience · doi:10.1038/nn.4067 · Cited by 472 · see citing works
Self-citation
The Synaptic Accumulation of Hyperphosphorylated Tau Oligomers in Alzheimer Disease Is Associated With Dysfunction of the Ubiquitin-Proteasome System
Tai, H., Serrano‐Pozo, A., Hashimoto, T., Frosch, M. P., Spires‐Jones, T. L., & Hyman, B. T. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.06.033 · Cited by 456 · see citing works
The role of astrocytes in amyloid production and Alzheimer's disease
Frost, G. R., & Li, Y. (2017) · Open Biology · doi:10.1098/rsob.170228 · Cited by 435 · see citing works
Tau association with synaptic vesicles causes presynaptic dysfunction
Zhou, L., McInnes, J., Wierda, K., Holt, M., Herrmann, A. G., Jackson, R. J., Wang, Y.-C., Swerts, J., Beyens, J., Miskiewicz, K., et al. (2017) · Nature Communications · doi:10.1038/ncomms15295 · Cited by 434 · see citing works
Frontotemporal dementia
Olney, N. T., Spina, S., & Miller, B. L. (2017) · Neurologic Clinics · doi:10.1016/j.ncl.2017.01.008 · Cited by 419 · see citing works
Apolipoprotein e sets the stage: response to injury triggers neuropathology
Mahley, R. W., & Huang, Y. (2012) · Neuron · doi:10.1016/j.neuron.2012.11.020 · Cited by 412 · see citing works
Glial contributions to neurodegeneration in tauopathies
Leyns, C. E. G., & Holtzman, D. M. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0192-x · Cited by 409 · see citing works
The complexity of tau in Alzheimer’s disease
Naseri, N. N., Wang, H., Guo, J. D., Sharma, M., & Luo, W. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.04.022 · Cited by 374 · see citing works
<scp>mTOR</scp> regulates tau phosphorylation and degradation: implications for Alzheimer's disease and other tauopathies
Caccamo, A., Magrì, A., Medina, D. X., Wisely, E. V., López‐Aranda, M. F., Silva, A. J., & Oddo, S. (2013) · Aging Cell · doi:10.1111/acel.12057 · Cited by 362 · see citing works
Tau interactome maps synaptic and mitochondrial processes associated with neurodegeneration
Tracy, T. E., Madero‐Pérez, J., Swaney, D. L., Chang, T. S., Moritz, M., Konràd, C., Ward, M. E., Stevenson, E. J., Hüttenhain, R., Kauwe, G., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.041 · Cited by 347 · see citing works
Alzheimer's disease as type 3 diabetes: common pathophysiological mechanisms between Alzheimer's disease and type 2 diabetes
Michailidis, M., Moraitou, D., Tata, D. A., Kalinderi, K., Papamitsou, T., & Papaliagkas, V. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052687 · Cited by 330 · see citing works
Fluid biomarkers for mild traumatic brain injury and related conditions
Zetterberg, H., & Blennow, K. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2016.127 · Cited by 328 · see citing works
Recent Advances in the Inhibition of p38 MAPK as a Potential Strategy for the Treatment of Alzheimer’s Disease
Lee, J. K., & Kim, N. (2017) · Molecules · doi:10.3390/molecules22081287 · Cited by 323 · see citing works
Mouse models of Alzheimer's disease
Hall, A. M., & Roberson, E. D. (2012) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2011.11.017 · Cited by 317 · see citing works
Role of Amyloid-β and Tau Proteins in Alzheimer’s Disease: Confuting the Amyloid Cascade
Gulisano, W., Maugeri, D., Baltrons, M. A., Fà, M., Amato, A., Palmeri, A., D’Adamio, L., Grassi, C., Devanand, D. P., Honig, L. S., et al. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179935 · Cited by 313 · see citing works
Microtubule-associated protein tau is essential for long-term depression in the hippocampus
Kimura, T., Whitcomb, D. J., Jo, J., Regan, P., Piers, T., Heo, S., Brown, C., Hashikawa, T., Murayama, M., Seok, H., et al. (2014) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2013.0144 · Cited by 307 · see citing works
Mechanisms of secretion and spreading of pathological tau protein
Brunello, C. A., Merezhko, M., Uronen, R.-L., & Huttunen, H. J. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03349-1 · Cited by 304 · see citing works
Physiological and pathological phosphorylation of tau by Cdk5
Kimura, T., Ishiguro, K., & Hisanaga, S. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00065 · Cited by 297 · see citing works
Autophagic degradation of tau in primary neurons and its enhancement by trehalose
Krüger, U., Wang, Y., Kumar, S., & Mandelkow, E.-M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.009 · Cited by 297 · see citing works
PI3-kinase/Akt/mTOR signaling: Impaired on/off switches in aging, cognitive decline and Alzheimer's disease
Neill, C. O. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.02.025 · Cited by 292 · see citing works
Amyloid-β oligomers induce synaptic damage via Tau-dependent microtubule severing by TTLL6 and spastin
Zempel, H., Luedtke, J., Kumar, Y., Biernat, J., Dawson, H., Mandelkow, E., & Mandelkow, E. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.207 · Cited by 283 · see citing works
Targeted degradation of aberrant tau in frontotemporal dementia patient-derived neuronal cell models
Silva, M. C., Ferguson, F. M., Cai, Q., Donovan, K. A., Nandi, G., Patnaik, D., Zhang, T., Huang, H.-T., Lucente, D. E., Dickerson, B. C., et al. (2019) · eLife · doi:10.7554/elife.45457 · Cited by 283 · see citing works
Tau Accumulation Causes Mitochondrial Distribution Deficits in Neurons in a Mouse Model of Tauopathy and in Human Alzheimer's Disease Brain
Kopeikina, K. J., Carlson, G. A., Pitstick, R., Ludvigson, A. E., Peters, A., Luebke, J. I., Koffie, R. M., Frosch, M. P., Hyman, B. T., & Spires‐Jones, T. L. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.07.004 · Cited by 272 · see citing works
Neuroinflammation in Alzheimer&rsquo;s disease
Zhang, F., & Jiang, L. (2015) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s75546 · Cited by 276 · see citing works
Antisense oligonucleotides: translation from mouse models to human neurodegenerative diseases
Schoch, K. M., & Miller, T. M. (2017) · Neuron · doi:10.1016/j.neuron.2017.04.010 · Cited by 274 · see citing works
“Under normal conditions, tau functions to stabilize microtubules and may also be involved in intracellular signaling, scaffolding, and neurogenesis (Morris et al., 2011).”
Lost after translation: missorting of Tau protein and consequences for Alzheimer disease
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Authors: Morris, M., Maeda, S., Vossel, K., & Mucke, L.
Affiliations: Gladstone Institutes (US)
Corresponding author: Mucke, Lennart
ORCID: Morris, Meaghan
Maeda, Sumihiro
Vossel, Keith
Mucke, Lennart
Venue: Neuron
Publisher: Elsevier BV
Published: 2011-05
Volume: 70
Issue: 3
Pages: 410-426
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/j.neuron.2011.04.009
PMC: PMC3319390
OpenAlex: W2125985978
Cited by: 899
References: 196
Citations by year: 2026: 29 · 2025: 33 · 2024: 36 · 2023: 52 · 2022: 59 · 2021: 65 · 2020: 59 · 2019: 59 · 2018: 72 · 2017: 65 · 2016: 67 · 2015: 70 · 2014: 67 · 2013: 80 · 2012: 59
FWCI: 7.63
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 808 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (AG011385, NS041787)
Tau Consortium
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords: tau protein, microtubule binding, cytoskeletal organization, signaling, neurodegenerative diseases, tauopathy
MeSH terms: Animals, Humans, Microtubules, Models, Biological, Signal Transduction, tau Proteins, Neurodegenerative Diseases

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