Caspase-2 cleavage of tau reversibly impairs memory
Abstract
In Alzheimer's disease (AD) and other tauopathies, the tau protein forms fibrils, which are believed to be neurotoxic. However, fibrillar tau has been dissociated from neuron death and network dysfunction, suggesting the involvement of nonfibrillar species. Here we describe a novel pathological process in which caspase-2 cleavage of tau at Asp314 impairs cognitive and synaptic function in animal and cellular models of tauopathies by promoting the missorting of tau to dendritic spines. The truncation product, Δtau314, resists fibrillation and is present at higher levels in brains from cognitively impaired mice and humans with AD. The expression of tau mutants that resisted caspase-2 cleavage prevented tau from infiltrating spines, dislocating glutamate receptors and impairing synaptic function in cultured neurons, and it prevented memory deficits and neurodegeneration in mice. Decreasing the levels of caspase-2 restored long-term memory in mice that had existing deficits. Our results suggest an overall treatment strategy for re-establishing synaptic function and restoring memory in patients with AD by preventing tau from accumulating in dendritic spines.
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Tau can be cleaved by caspase-1, 2, 3, 6 and 7 in vitro.
“Although tau can be cleaved by caspase-1, 2, 3, 6 and 7 in vitro”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [190]
Caspase-2 cleaves tau at Asp314.
“Caspase-2 cleaves tau at Asp314”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [190]
Increased levels of truncated tau-314 have been described in AD brain.
“increased levels of truncated tau-314 have been described in AD brain.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [190]
Only caspase-2, 3 and 6 cleaved tau products have been linked to AD.
“only caspase-2, 3 and 6 cleaved tau products have been linked to AD [190–193].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [190]
Downregulation of caspase-2 partially rescues memory deficits in rTg4510 tau transgenic mice.
“Indeed, downregulation of caspase-2 partially rescues memory deficits in rTg4510 tau transgenic mice [190].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [190]
Tau-314 dissociates from microtubules and promotes distribution of full-length tau and tau-314 to dendritic spines to induce synaptic and cognitive dysfunction.
“Tau-314 dissociates from microtubules and promotes the distribution of full-length tau and tau-314 to dendritic spines to induce synaptic and cognitive dysfunction.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [190]
Cites
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 · see citing works
Self-citationRetractedAmyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208 · see citing works
Tau-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 · see citing works
Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function
SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014 · see citing works
Self-citationDendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821 · see citing works
MEROPS: the database of proteolytic enzymes, their substrates and inhibitors
Rawlings, N. D., Barrett, A. J., & Bateman, A. G. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr987 · Cited by 1,539 · see citing works
Liao, D., Hessler, N. A., & Malinow, R. (1995) · Nature · doi:10.1038/375400a0 · Cited by 1,365 · see citing works
Old, new and emerging functions of caspases
Shalini, S., Dorstyn, L., Dawar, S., & Kumar, S. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.216 · Cited by 1,267 · see citing works
Evidence for silent synapses: Implications for the expression of LTP
Isaac, J. T. R., Nicoll, R. A., & Malenka, R. C. (1995) · Neuron · doi:10.1016/0896-6273(95)90046-2 · Cited by 1,233 · see citing works
Tau pathology and neurodegeneration
Spillantini, M. G., & Goedert, M. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70090-5 · Cited by 1,133 · see citing works
Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., Pitstick, R., Carlson, G. A., Lanier, L. M., Yuan, L.-L., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.030 · Cited by 1,118 · see citing works
Self-citationDifferential Regulation of Dynein and Kinesin Motor Proteins by Tau
Dixit, R., Ross, J. L., Goldman, Y. E., & Holzbaur, E. L. F. (2008) · Science · doi:10.1126/science.1152993 · Cited by 1,012 · see citing works
MEROPS : the database of proteolytic enzymes, their substrates and inhibitors
Rawlings, N. D., Waller, M., Barrett, A. J., & Bateman, A. G. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt953 · Cited by 870 · see citing works
Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease
Gamblin, T. C., Chen, F., Zambrano, A., Abraha, A., Lagalwar, S., Guillozet, A. L., Lu, M., Fu, Y., Garcia-Sierra, F., LaPointe, N., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630428100 · Cited by 831 · see citing works
The Relationship between Aβ and Memory in the Tg2576 Mouse Model of Alzheimer's Disease
Westerman, M. A., Cooper-Blacketer, D., Mariash, A., Kotilinek, L., Kawarabayashi, T., Younkin, L. H., Carlson, G. A., Younkin, S. G., & Ashe, K. H. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-05-01858.2002 · Cited by 714 · see citing works
Self-citationRamsden, M., Kotilinek, L., Forster, C., Paulson, J., McGowan, E., SantaCruz, K., Guimaraes, A., Yue, M., Lewis, J., Carlson, G., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.3279-05.2005 · Cited by 702 · see citing works
Self-citationZempel, H., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.2357-10.2010 · Cited by 686 · see citing works
Defects in regulation of apoptosis in caspase-2-deficient micePreprint
Bergeron, L., Perez, G. I., MacDonald, G., Shi, L., Sun, Y., Jurisicova, A., Varmuza, S., Latham, K. E., Flaws, J. A., Salter, J. C. M., et al. (1998) · Genes & Development · doi:10.1101/gad.12.9.1304 · Cited by 681 · see citing works
IRE1α Cleaves Select microRNAs During ER Stress to Derepress Translation of Proapoptotic Caspase-2
Upton, J.-P., Wang, L., Han, D., Wang, E. S., Huskey, N. E., Lim, L., Truitt, M., McManus, M. T., Ruggero, D., Goga, A., et al. (2012) · Science · doi:10.1126/science.1226191 · Cited by 640 · see citing works
Kumar, S., Kinoshita, M., Noda, M., Copeland, N. G., & Jenkins, N. A. (1994) · Genes & Development · doi:10.1101/gad.8.14.1613 · Cited by 595 · see citing works
Neuronal activity regulates extracellular tau in vivo
Yamada, K., Holth, J. K., Liao, F., Stewart, F. R., Mahan, T. E., Jiang, H., Cirrito, J. R., Patel, T. K., Hochgräfe, K., Mandelkow, E., et al. (2014) · The Journal of Experimental Medicine · doi:10.1084/jem.20131685 · Cited by 574 · see citing works
Caspase activation precedes and leads to tangles
de Calignon, A., Fox, L. M., Pitstick, R., Carlson, G. A., Bacskai, B. J., Spires-Jones, T. L., & Hyman, B. T. (2010) · Nature · doi:10.1038/nature08890 · Cited by 517 · see citing works
Zhang, Z., Song, M., Liu, X., Kang, S. S., Kwon, I.-S., Duong, D. M., Seyfried, N. T., Hu, W. T., Liu, Z., Wang, J.-Z., et al. (2014) · Nature Medicine · doi:10.1038/nm.3700 · Cited by 494 · see citing works
Clinical and pathological correlates of apolipoprotein E ε4 in Alzheimer's disease
Gomez‐Isla, T., West, H. L., Rebeck, G. W., Harr, S. D., Growdon, J. H., Locascio, J. J., Perls, T. T., Lipsitz, L. A., & Hyman, B. T. (1996) · Annals of Neurology · doi:10.1002/ana.410390110 · Cited by 378 · see citing works
C-terminal inhibition of tau assembly in vitro and in Alzheimer’s disease
Abraha, A., Ghoshal, N., Gamblin, T. C., Cryns, V. L., Berry, R. W., Kuret, J., & Binder, L. I. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.21.3737 · Cited by 326 · see citing works
Tau pathophysiology in neurodegeneration: a tangled issue
Spires‐Jones, T. L., Stoothoff, W. H., de Calignon, A., Jones, P., & Hyman, B. T. (2009) · Trends in Neurosciences · doi:10.1016/j.tins.2008.11.007 · Cited by 317 · see citing works
Wang, X., Zhao, Y., Zhang, X., Badie-Mahdavi, H., Zhou, Y., Mu, Y., Loo, L. S., Cai, L., Thompson, R. C., Yang, B., et al. (2013) · Nature Medicine · doi:10.1038/nm.3117 · Cited by 241 · see citing works
Tau-Mediated Cytotoxicity in a Pseudohyperphosphorylation Model of Alzheimer's Disease
Fath, T., Eidenmüller, J., & Brandt, R. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-22-09733.2002 · Cited by 233 · see citing works
The Role of Caspase Cleavage of Tau in Alzheimer Disease Neuropathology
Cotman, C. W., Poon, W. W., Rissman, R. A., & Blurton-Jones, M. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.104 · Cited by 199 · see citing works
Fasulo, L., Ugolini, G., Visintin, M., Bradbury, A. M., Brancolini, C., Verzillo, V., Novák, M., & Cattaneo, A. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750624.x · Cited by 195 · 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
Pathological Tau Disrupts Ongoing Network Activity
Menkes-Caspi, N., Yamin, H. G., Kellner, V., Spires-Jones, T. L., Cohen, D., & Stern, E. A. (2015) · Neuron · doi:10.1016/j.neuron.2015.01.025 · Cited by 184 · see citing works
A Caspase Cleaved Form of Tau Is Preferentially Degraded through the Autophagy Pathway
Dolan, P. J., & Johnson, G. V. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.110940 · Cited by 147 · see citing works
Wang, Y., Garg, S., Mandelkow, E., & Mandelkow�, E. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380955 · Cited by 140 · see citing works
Miller, E. C., Teravskis, P. J., Dummer, B. W., Zhao, X., Huganir, R. L., & Liao, D. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12507 · Cited by 131 · see citing works
Self-citationExtended analysis of path data from mutant mice using the public domain software Wintrack
Wolfer, D. P., Madani, R., Valenti, P., & Lipp, H. (2001) · Physiology & Behavior · doi:10.1016/s0031-9384(01)00531-5 · Cited by 130 · see citing works
Synaptic alterations in the rTg4510 mouse model of tauopathy
Kopeikina, K. J., Polydoro, M., Tai, H., Yaeger, E., Carlson, G. A., Pitstick, R., Hyman, B. T., & Spires‐Jones, T. L. (2012) · The Journal of Comparative Neurology · doi:10.1002/cne.23234 · Cited by 125 · see citing works
Caspase-2 is required for dendritic spine and behavioural alterations in J20 APP transgenic mice
Pozueta, J., Lefort, R., Ribé, E. M., Troy, C. M., Arancio, O., & Shelanski, M. L. (2013) · Nature Communications · doi:10.1038/ncomms2927 · Cited by 100 · see citing works
A nonapoptotic role for CASP2/caspase 2
Tiwari, M., Sharma, L. K., Vanegas, D., Callaway, D. A., Bai, Y., Lechleiter, J. D., & Herman, B. A. (2014) · Autophagy · doi:10.4161/auto.28528 · Cited by 75 · see citing works
Effect Size of Memory Deficits in Mice with Adult-Onset P301L Tau Expression
Hunsberger, H. C., Rudy, C. C., Weitzner, D., Zhang, C., Tosto, D. E., Knowlan, K., Xu, Y., & Reed, M. N. (2014) · Behavioural Brain Research · doi:10.1016/j.bbr.2014.06.057 · Cited by 46 · see citing works
Caspase-2 protects against oxidative stress in vivo
Shalini, S., Puccini, J., Wilson, C. H., Finnie, J. W., Dorstyn, L., & Kumar, S. (2014) · Oncogene · doi:10.1038/onc.2014.413 · Cited by 37 · see citing works
Carroll, J. B., Southwell, A. L., Graham, R. K., Lerch, J. P., Ehrnhoefer, D. E., Cao, L., Zhang, W.-N., Deng, Y., Bissada, N., Henkelman, R. M., et al. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-59 · Cited by 35 · see citing works
Caspase-Mediated Truncation of Tau Potentiates Aggregation
Lee, S., & Shea, T. B. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/731063 · Cited by 25 · see citing works
Characterization and Use of Monoclonal Antibodies to Tau and Paired Helical Filament Tau
Davies, P. (2003) · Humana Press eBooks · doi:10.1385/1-59259-195-7:361 · Cited by 19 · see citing works
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BackgroundDejanovic, B., Huntley, M. A., De Mazière, A., Meilandt, W. J., Wu, T., Srinivasan, K., Jiang, Z., Gandham, V., Friedman, B. A., Ngu, H., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.10.014 · Cited by 575 · see citing works
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- Authors
- Zhao, X., Kotilinek, L. A., Smith, B., Hlynialuk, C., Zahs, K., Ramsden, M., Cleary, J., & Ashe, K. H.
- Affiliations
- University of Minnesota (US)
- Corresponding author
- Ashe, Karen H
- Venue
- Nature Medicine
- Published
- 2016-10-10
- Volume
- 22
- Issue
- 11
- Pages
- 1268-1276
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- OpenAlex
- W2530330371
- Cited by
- 187
- References
- 45
- Citations by year
- 2026: 14 · 2025: 7 · 2024: 13 · 2023: 26 · 2022: 19 · 2021: 24 · 2020: 21 · 2019: 26 · 2018: 21 · 2017: 14 · 2016: 2
- FWCI
- 16.89
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Medicine (publishedVersion, public-domain)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (R01AG017917)
- National Institute of Neurological Disorders and Stroke (R01NS063214, R01NS079374)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- caspase-2, tau protein, tau cleavage, tauopathy, Alzheimer's disease, dendritic spines, synaptic dysfunction, memory impairment, neurodegeneration, cognitive impairment
- MeSH terms
- Alzheimer Disease, Animals, Cells, Cultured, Disease Models, Animal, Hippocampus, Humans, Memory, Memory Disorders, Mice, Transgenic, Neurons, Organ Size, Synapses, Blotting, Western, tau Proteins, Receptors, Glutamate, Excitatory Postsynaptic Potentials, Reverse Transcriptase Polymerase Chain Reaction, Caspases, Dendritic Spines, Mice, Caspase 2, Morpholinos
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