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Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing
Open accessAbstract
Aggregation and cleavage are two hallmarks of Tau pathology in Alzheimer disease (AD), and abnormal fragmentation of Tau is thought to contribute to the nucleation of Tau paired helical filaments. Clearance of the abnormally modified protein could occur by the ubiquitin-proteasome and autophagy-lysosomal pathways, the two major routes for protein degradation in cells. There is a debate on which of these pathways contributes to clearance of Tau protein and of the abnormal Tau aggregates formed in AD. Here, we demonstrate in an inducible neuronal cell model of tauopathy that the autophagy-lysosomal system contributes to both Tau fragmentation into pro-aggregating forms and to clearance of Tau aggregates. Inhibition of macroautophagy enhances Tau aggregation and cytotoxicity. The Tau repeat domain can be cleaved near the N terminus by a cytosolic protease to generate the fragment F1. Additional cleavage near the C terminus by the lysosomal protease cathepsin L is required to generate Tau fragments F2 and F3 that are highly amyloidogenic and capable of seeding the aggregation of Tau. We identify in this work that components of a selective form of autophagy, chaperone-mediated autophagy, are involved in the delivery of cytosolic Tau to lysosomes for this limited cleavage. However, F1 does not fully enter the lysosome but remains associated with the lysosomal membrane. Inefficient translocation of the Tau fragments across the lysosomal membrane seems to promote formation of Tau oligomers at the surface of these organelles which may act as precursors of aggregation and interfere with lysosomal functioning.
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“Disruption of the autophagy-lysosomal pathway (ALP) is another pathological hallmark in human tauopathy brain (Bain et al., 2019; Piras et al., 2016; Wang et al., 2009).”
From ELAVL4, splicing, and glutamatergic dysfunction precede neuron loss in MAPT mutation cerebral organoids (2021) · cites this paper as Wang et al., 2009
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“Cumulative evidence from murine tauopathy models and postmortem patient brain studies suggests that early tau post-translational modifications lead to misfolding, mislocalization, oligomerization, and changes in solubility. These events appear to be determinant toxicity effectors”
From Targeted degradation of aberrant tau in frontotemporal dementia patient-derived neuronal cell models (2019) · cites this paper as Wang et al., 2009
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Citations
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Sampaio‐Marques, B., & Ludovico, P. (2015) · Biomolecules · doi:10.3390/biom5020735 · Cited by 15
“alterations on lysosome degradation processes, which is also supported by observations in the brain of Alzheimer’s disease patients, where a deficiency in SIRT1 leads to hyperacetylation of the phosphorylated tau, resulting in impaired tau degradation by the 26S proteasome [146] and by autophagy [147].”
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Zeng, P. H., Liu, Y.-C., Wang, X., Ye, C., Sun, Y., Su, H.-F., Qiu, S.-W., Li, Y., Wang, Y., Wang, Y., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1013891 · Cited by 17
“The degradation of tau mainly occurs via the ubiquitin-proteasome pathway and the lysosomal proteolysis pathway, and inhibition of these pathways promote tau aggregation (Wang et al., 2009).”
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Disease-modifying strategies in primary tauopathies
Rösler, T. W., Costa, M., & Höglinger, G. U. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.107842 · Cited by 16
HMGCS2-Induced Autophagic Degradation of Tau Involves Ketone Body and ANKRD24
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“However, subsequent studies demonstrate that inhibition of the proteasomes by lactacystin does not change Tau levels in cultured primary neurons or SH-SY5Y cells, in the presence or absence of cyclo-heximide for 24 h [73, 74].”
Davis, S. E., Cook, A. K., Hall, J. A., Voskobiynyk, Y., Carullo, N. V. N., Boyle, N. R., Hakim, A. R., Anderson, K. M., Hobdy, K. P., Pugh, D. A., et al. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01571-4 · Cited by 12
“Lysosomal dysfunction may be an important contributor to FTLDTDP and FTLD-tau pathogenesis, as the endolysosomal and autophagy-lysosomal pathways clear TDP-43 and tau, and disruption of these pathways exacerbates both types of pathology [12, 53, 54, 78, 88, 89, 96].”
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Bejarano, E., Domenech‐Bendaña, A., Avila-Portillo, N., Rowan, S., Edirisinghe, S., & Taylor, A. (2024) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2024.101260 · Cited by 15
Internalization of extracellular Tau oligomers in Alzheimer’s disease
Chinnathambi, S., Rangappa, N., & Chandrashekar, M. (2025) · Advances in clinical chemistry · doi:10.1016/bs.acc.2025.01.005 · Cited by 14
Ibarra-Bracamontes, V., Escobar‐Herrera, J., Krištofíková, Z., Řı́pová, D., Florán, B., & García‐Sierra, F. (2020) · Brain Research · doi:10.1016/j.brainres.2020.146953 · Cited by 14
Domenico, F. D., Zuliani, I., & Tramutola, A. (2019) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1691919 · Cited by 13
“Moreover, macroautophagy inhibition by 3-metyhladenine implicates tau enhanced aggregation and cytotoxicity, demonstrating a pivotal role of autophagy in preventing the formation of tau tangles [49].”
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“Indeed, alterations in both pathways have been linked to AD [11, 12].”
BackgroundRegulation of autophagy by amino acid availability in S. cerevisiae and mammalian cells
Abeliovich, H. (2014) · Amino Acids · doi:10.1007/s00726-014-1787-y · Cited by 13
“…identified a role for CMA in aging (Cuervo and Dice 2000; Kiffin et al. 2007), neurodegenerative disease (Cuervo et al. 2004; Mak et al. 2010; MartinezVicente et al. 2008; Orenstein et al. 2013; Vogiatzi et al. 2008; Wang et al. 2009; Liu et al. 2009), and cancer (Kon et al. 2011; Lv et al. 2011).”
BackgroundProtein quality control—linking the unfolded protein response to disease
Cyr, D., & Hebert, D. N. (2009) · EMBO Reports · doi:10.1038/embor.2009.224 · Cited by 16
“Such an event could explain the apparent links between ER stress and the cytosolic stress response (Mu et al, 2008). activation of the transcription factor ATF4.”
InfluentialAn AMPK-dependent regulatory pathway in tau-mediated toxicity
Galasso, A., Cameron, C. S., Frenguelli, B. G., & Moffat, K. G. (2017) · Biology Open · doi:10.1242/bio.022863 · Cited by 13
“Additionally, defects in autophagy lead to an increased accumulation of tau phosphorylated at the KXGS motifs (Wang et al., 2009), such as Ser-262, species reported to be also less susceptible to proteasomal degradation mediated by Hsp90 (Dickey et al.”
InfluentialYang, C., Li, X., Zhang, L., Li, Y., Li, L., & Zhang, L. (2019) · Journal of Natural Medicines · doi:10.1007/s11418-019-01318-3 · Cited by 13
Cathepsin D: A Candidate Link between Amyloid ?-protein and Tauopathy in Alzheimer Disease
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“Previous research into the physiology or diseases associated with LAMP-2 primarily focused on aging [69], renal hypertrophy [70], and neurodegenerative diseases such as Parkinson’s disease [71,72] and Alzheimer’s disease [73,74].”
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Chaperone-mediated autophagy as a modulator of aging and longevity
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The Fate of Tau Aggregates Between Clearance and Transmission
Seitkazina, A., Kim, K. H., Fagan, E., Sung, Y., Kim, Y. K., & Lim, S. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.932541 · Cited by 10
“Hsc70 mediates the sorting of tau proteins to lysosomes or late-endosomes (Wang et al., 2009).”
BackgroundFan, Y., Wang, Z., & He, D. (2022) · Current Neuropharmacology · doi:10.2174/1570159x20666220817140737 · Cited by 11
“Activation of autophagy promoted the degradation of insoluble tau and protected against its toxicity in Drosophila [193]. mTOR-independent activation of autophagy also facilitated neuronal survival by reducing the aggregation of tau in the brains of human tauopathy model mice [194].”
“Dirty Dancing” of Calcium and Autophagy in Alzheimer’s Disease
Zhang, H., & Борисович, Б. И. (2023) · Life · doi:10.3390/life13051187 · Cited by 11
“Tau phosphorylated at the KXGS motifs of the repeat domain, which cannot be degraded by the UPS, is efficiently degraded by autophagy [77].”
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“In AD brain tissue, Hsc70 associates with neurofibrillary tangles indicating that the CMA system is also involved in the degradation of neurofibrillary tangles (Wang et al., 2009).”
BackgroundCerebrospinal fluid endo-lysosomal proteins as potential biomarkers for Huntington’s disease
Lowe, A. J., Sjödin, S., Rodrigues, F. B., Byrne, L. M., Blennow, K., Tortelli, R., Zetterberg, H., & Wild, E. J. (2020) · PLoS ONE · doi:10.1371/journal.pone.0233820 · Cited by 11
Targeting Chaperone-Mediated Autophagy for Disease Therapy
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Autophagy mediates proteolysis of NPM1 and HEXIM1 and sensitivity to BET inhibition in AML cells
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“Alternatively, the autophagy–lysosomal pathway may cause the accumulation of tau fragments prone to aggregation [29].”
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“In addition, Tau has importance in maintaining an appropriate morphology of neurons and it appear to modulate axonal transport [26, 27].”
BackgroundDevelopment of AD-Like Pathology in Skeletal Muscle
Chen, X., Miller, N. M., Afghah, Z., & Geiger, J. D. (2019) · Journal of Parkinson’s Disease and Alzheimer’s Disease · doi:10.13188/2376-922x.1000028 · Cited by 10
“Given that tau aggregates can be degraded by cathepsin D in autophagosomes-lysosomes [170-174], impaired lysosome degradation could lead to tau aggregation and the development of neurofibrillary tangle.”
BackgroundSiano, G., Micaelli, M., Scarlatti, A., Quercioli, V., Primio, C. D., & Cattaneo, A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.569395 · Cited by 10
“These aggregates resulted in K114 positive showing an amyloidogenic structure, however, since the 336QVEVK340 sequence targets Tau for degradation via chaperone-mediated autophagy (Wang et al., 2009) we cannot exclude the partial contribution of Tau accumulation at lysosomes for the aggregation induction.”
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“The second pathway involves chaperone-mediated autophagy (CMA) which is responsible for clearance of multiple intracellular proteins with a specific motif including tau [114, 115, 119–121].”
Lysosome pH Dynamics in Physiology and Disease: Molecular Mechanisms and Therapeutic Insights
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“Tau has also been observed within autophagic vesicles and accumulated in autolysosomes when degradation is compromised 77,78 .”
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“Future investigation will determine which proteostasis pathways – UPS, ALP or UPR – participate in TDP-43 enhancement of Dendra2::tau alone.”
InfluentialArgentati, C., Tortorella, I., Bazzucchi, M., Emiliani, C., Morena, F., & Martino, S. (2020) · Journal of Personalized Medicine · doi:10.3390/jpm10030115 · Cited by 10
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Heat Shock Proteins and Protein Quality Control in Alzheimer’s Disease
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“Moreover, tau is also degraded by autophagy (Wang et al., 2009; Krüger et al., 2012; Lee et al., 2013; Neu et al., 2025).”
The role of amyloid β in the pathological mechanism of GNE myopathy
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Aging-associated REGγ proteasome decline predisposes to tauopathy
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“Excessive soluble neurotoxic tau proteins can be degraded through the UPS (49), chaperon-mediated autophagy (50), and endosomal microautophagy (51).”
BackgroundXie, M., Shi, R., Pan, Y., Zeng, T., Chen, Q.-C., Wang, S., & Liao, X. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8702-0 · Cited by 7
The Cascade of Oxidative Stress and Tau Protein Autophagic Dysfunction in Alzheimer’s Disease
Liu, Z., Li, P., Wu, J., Wang, Y., Li, P., Hou, X., Zhang, Q., Wei, N., Zhao, Z., Liang, H., et al. (2015) · InTech eBooks · doi:10.5772/59980 · Cited by 9
Grenon, M. B., Papavergi, M.-T., Bathini, P., Sadowski, M. J., & Lemere, C. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25115754 · Cited by 7
“Disrupted lysosome function leads to reduced A β and tau clearance, triggering a cascade of downstream events such as neuroinflammation, synaptic plasticity deficits, and cellular stress, consequently contributing to neuritic dystrophy and neurode-generation [65,161,162].”
BackgroundYin, P., Wang, H., Xue, T., Yu, X., Meng, X., Mi, Q., Song, S., Xiong, B., Bi, Y., & Yu, L. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c00181 · Cited by 7
Mohamed, R. A., Abdallah, D. M., & El-Abhar, H. S. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01754-6 · Cited by 9
“In this regard, a prior study chronicled that amyloidogenic precursor protein (APP) and p -Tau, which are pivotal in the etiopathogenesis of AD, harbor KFERQ motifs, an attribute that facilitates their binding to LAMP2A to be marked for proteolytic degradation via CMA (Wang et al. 2009).”
Molecular hallmarks of neurodegeneration in polyglutamine spinocerebellar ataxias
Nóbrega, C., Marcelo, A., Rajado, A. T., Conceição, A., Estevam, B., Matos, C. A., Brito, D. V. C., Afonso, I. T., Codêsso, J. M., Koppenol, R., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08154-2 · Cited by 9
Syk inhibitors reduce tau protein phosphorylation and oligomerization
Yamaguchi, T., Hamano, T., Sada, K., Asano, R., Kanaan, N. M., Sasaki, H., Yen, S.-H. C., Kitazaki, Y., Endo, Y., Enomoto, S., et al. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106656 · Cited by 7
“Tau is degraded via autophagy (Hamano 2008; Wang et al., 2009).”
BackgroundCdks Regulate Autophagy via Vps34
Rubinsztein, D. C. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.05.013 · Cited by 7
“Since Cdk5 activation can block autophagy, and tau is an autophagy substrate, which accumulates and aggregates when this process is impaired (Wang et al., 2009), Cdk5 hyperactivation may also contribute to tau pathology by interfering with its clearance.”
BackgroundGozes, I. (2010) · The EPMA Journal · doi:10.1007/s13167-010-0029-y · Cited by 7
“In this respect, it has been suggested that tau fragments across the lysosomal membrane promote formation of tau oligomers at the surface of these organelles which may act as precursors of aggregation and interfere with lysosomal functioning [139].”
BackgroundChen, X., Liang, H., Soliman, M. L., & Geiger, J. D. (2014) · Journal of Parkinson’s Disease and Alzheimer’s Disease · doi:10.13188/2376-922x.1000002 · Cited by 7
Commentary: BAG3 as a Mediator of Endosome Function and Tau Clearance
Lin, H., Deaton, C. A., & Johnson, G. V. W. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.05.002 · Cited by 7
Xu, S., Liu, K., Qian, S., Wu, J., Hu, J., Zhou, D., & Zheng, T. (2025) · Neurochemistry International · doi:10.1016/j.neuint.2025.105976 · Cited by 6
Caughey, B. W., Artikis, E., Shoup, D. W., Orru, C. D., Alam, P., Parveen, S., King, S., Soukup, J., Hughson, A. G., & Priola, S. A. (2025) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00007-25 · Cited by 8
“Notably, PrP Sc (267), tau (268), and/or aSyn (269) fibrils can induce lysoso mal dysfunction, for example, leakage (270, 271), and their degradation products can affect mitochondria (272, 273).”
Severe neurodegeneration in brains of transgenic rats producing human tau prions
Ayers, J. I., Lopez, T. P., Steele, I. T., Oehler, A., Roman-Albarran, R., Cleveland, E., Chong, A., Carlson, G. A., Condello, C., & Prusiner, S. B. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02771-5 · Cited by 7
“Recent studies by others have demonstrated that misfolded hTau may be degraded by protein-clearance mechanisms [16, 38, 75].”
Sensing Protein Structural Transitions with Microfluidic Modulation Infrared Spectroscopy
Lucas, L., Tsoi, P. S., Nair, A., Ferreon, A. C. M., & Ferreon, J. C. (2025) · Biosensors · doi:10.3390/bios15060382 · Cited by 6
“In the cellular context, late endosomes and lysosomes maintain acidic pH values of ~4.5–5.5; under these acidic conditions, Tau may lose secondary structures, prior to proteolytic processing or aggregation [72].”
InfluentialChen, X., Wagener, J. F., Ghribi, O., & Geiger, J. D. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00129 · Cited by 6
“…of LDL cholesterol could encourage the accumulation of AβPP in endolysosomes by either promoting AβPP internalization (Waldron et al., 2006, 2008; Klug et al., 2011) or impairing the recycling of internalized AβPP back to plasma membrane (Andersen et al., 2005; Willnow and Andersen, 2013).”
BackgroundPhysiology of cellular demise: Apoptosis, necrosis, and autophagy
Kaur, D., & Deshmukh, R. R. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815762-6.00002-0 · Cited by 10
Transcriptomic signature of Alzheimer’s disease tau seed-induced pathology
Csicsatkova, N., Szalay, P., Matyasova, K., Mate, V., Cente, M., Smolek, T., Brezováková, V., Kawecka, L., Žilka, N., & Jadhav, S. (2021) · General Physiology and Biophysics · doi:10.4149/gpb_2021022 · Cited by 6
“This molecular association indicates the clearance of tau aggregates through lysosomal pathway and chaperonemediated autophagy (Wang et al. 2009; Abisambra et al. 2013).”
Hamano, T., & Endo, Y. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-89906-2.00006-x · Cited by 7
Zhang, K. K., Zhang, P., Kodur, A., Ertürk, İ., Burns, C. M., Kenyon, C. J., Miller, R. A., & Endicott, S. J. (2023) · Aging · doi:10.18632/aging.204796 · Cited by 7
Rosenzweig-Lipson, S. J. (2023) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2023.106 · Cited by 6
“Tau contains a KFERQ motif and Wang et al. demonstrated that degradation of wild type tau is CMA-dependent (94).”
BackgroundInfluentialCathepsin D in a Murine Model of Frontotemporal Dementia with Parkinsonism-Linked to Chromosome 17
Fernández-Montoya, J., & Pérez, M. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-140456 · Cited by 6
“Although clearance probably occurs through different mechanisms, there are some experimental evidences supporting tau degradation in lysosomes [7–9] and thus [10].”
Kim, B., Jang, T., Yoo, S., Lee, J. M., & Kim, E. (2021) · The FASEB Journal · doi:10.1096/fj.202001371rr · Cited by 6
Atsmon‐Raz, Y., & Miller, Y. (2015) · Israel Journal of Chemistry · doi:10.1002/ijch.201400162 · Cited by 6
George, J., Shafiq, K., Kapadia, M., Kalia, L. V., & Kalia, S. K. (2024) · Scientific Reports · doi:10.1038/s41598-024-64131-3 · Cited by 5
Axon Injury-Induced Autophagy Activation Is Impaired in a C. elegans Model of Tauopathy
Ko, S. H., Gonzalez, G., Liu, Z., & Chen, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228559 · Cited by 5
“To test whether injury-induced autophagy is affected by protein aggregation, we investigated autophagy dynamics in a transgenic Tau aggregation model that expresses chromosomally integrated versions of the amyloidogenic F3DK280 fragment of human Tau derived from the repeat domain of TauDK280 [31,33,34].”
BackgroundZhiyan, C., Min, Z., Yida, D., He, C., Hu, X., Yutong, L., Huan, W., & Sun, L. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1424803 · Cited by 5
Yakovlev, A. A., Kvichansky, A. A., Лыжин, А. А., Хаспеков, Л. Г., & Gulyaeva, N. V. (2013) · Neurochemical Journal · doi:10.1134/s1819712413020098 · Cited by 5
Role of Protein Ubiquitination and its Functional Importance
Wang, X., Wei, X., & Zhang, H. (2015) · Scientia Sinica Vitae · doi:10.1360/n052015-00065 · Cited by 4
The Lysosome in Aging‐Related Neurodegenerative Diseases
Nixon, R. A. (2016) · Wiley eBooks · doi:10.1002/9781118978320.ch9 · Cited by 5
Hernández-Díaz, S., Martinez-Olondo, P., Sanchez-Mirasierra, I., Montecinos-Oliva, C., Ghimire, S., Sutherland, J. D., Barrio, R., & Soukup, S. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.04.547658 · Cited by 5
“Evidence supports that Tau is degraded, at least partially, by macroautophagy 62 .”
Sahu, M., Seth, I., George, S. J., & Maitra, U. (2024) · Chemistry of Materials · doi:10.1021/acs.chemmater.4c01125 · Cited by 4
Islam, M., Karim, M. R. U., Argueta, E., Selim, M. N., Wojcikiewicz, E. P., & Du, D. (2025) · Membranes · doi:10.3390/membranes15070208 · Cited by 4
“Previous studies suggest that tau fragments, generated by proteolytic cleavage, remain associated with intracellular membranes [31].”
Targeted tau protein degradation: a promising therapeutic approach for tauopathies
Baazaoui, N., Alfaifi, M. Y., Shati, A. A., Saad, R. B., & Garzoli, S. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.11.041 · Cited by 5
Binas, S., Mardani, M., Siahtiri, S., & Nejad, A. M. (2025) · ASME Open Journal of Engineering · doi:10.1115/1.4068905 · Cited by 4
Bourdenx, M., & Dehay, B. (2017) · médecine/sciences · doi:10.1051/medsci/20173303013 · Cited by 5
Metadata
- Authors
- Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E.
- Affiliations
- Max Planck Unit for Structural Molecular Biology (DE)
- Albert Einstein College of Medicine (US)
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2009-08-04
- Volume
- 18
- Issue
- 21
- Pages
- 4153-4170
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- PMC
- PMC2758146
- OpenAlex
- W2133548029
- Cited by
- 617
- References
- 72
- Citations by year
- 2026: 25 · 2025: 35 · 2024: 30 · 2023: 28 · 2022: 38 · 2021: 43 · 2020: 45 · 2019: 34 · 2018: 37 · 2017: 32 · 2016: 41 · 2015: 41 · 2014: 28 · 2013: 30 · 2012: 45
- FWCI
- 28.59
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Human Molecular Genetics (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Funders
- National Institute on Aging (P01AG031782, AG031782)
- National Institute of Neurological Disorders and Stroke (NS038370, P50NS038370)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, tau aggregation, lysosomal processing, autophagy-lysosome pathway, chaperone-mediated autophagy, cathepsin L, macroautophagy, Alzheimer's disease, tauopathy, lysosomal membrane, tau oligomers, protein clearance
- MeSH terms
- Animals, Autophagy, Humans, Lysosomes, Microtubule-Associated Proteins, Models, Biological, Mutation, Peptide Fragments, Phagosomes, Protein Binding, Blotting, Western, tau Proteins, Protein Transport, Tauopathies, Cell Line, Tumor, HSC70 Heat-Shock Proteins, Mice, Protein Multimerization, Cathepsin L
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