Acetylated tau inhibits chaperone-mediated autophagy and promotes tau pathology propagation in mice
Open accessAbstract
Disrupted homeostasis of the microtubule binding protein tau is a shared feature of a set of neurodegenerative disorders known as tauopathies. Acetylation of soluble tau is an early pathological event in neurodegeneration. In this work, we find that a large fraction of neuronal tau is degraded by chaperone-mediated autophagy (CMA) whereas, upon acetylation, tau is preferentially degraded by macroautophagy and endosomal microautophagy. Rerouting of acetylated tau to these other autophagic pathways originates, in part, from the inhibitory effect that acetylated tau exerts on CMA and results in its extracellular release. In fact, experimental blockage of CMA enhances cell-to-cell propagation of pathogenic tau in a mouse model of tauopathy. Furthermore, analysis of lysosomes isolated from brains of patients with tauopathies demonstrates similar molecular mechanisms leading to CMA dysfunction. This study reveals that CMA failure in tauopathy brains alters tau homeostasis and could contribute to aggravate disease progression.
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The balance between cell proliferation and programmed cell death is altered in LSDs as well as neurodegenerative disorders.
“The balance between cell proliferation and programmed cell death is altered in LSDs as well as neurodegenerative disorders.26,27”
From The lysosome and proteostatic stress at the intersection of pediatric neurological disorders and adult neurodegenerative diseases (2025) · cites this paper as [27]
The Results section, “CMA dynamics are altered in AD patient brains” (page unavailable), reports impaired chaperone-mediated autophagy in Alzheimer’s disease, not a change in the balance between cell proliferation and programmed cell death. Searches for that balance, apoptosis, and lysosomal storage disorders found no passage in our copy addressing the claim. (LLM, conf=0.76)
Experimental — accuracy not yet measuredAcetylation of tau is an early pathological feature of neurodegeneration; acetylated tau inhibits its degradation, promotes pathological aggregation and propagation, and contributes to tauopathy.
“In addition, the acetylation of tau is an early pathological feature of neurodegeneration. Acetylated tau inhibits its degradation, promotes pathological aggregation and propagation, and contributes to tauopathy [46–51].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [50]
Blockage of CMA leads to rerouting of some pathogenic forms of MAPT/tau toward endosomal microautophagy, promoting fusion of late endosomes with the plasma membrane and subsequent extraneuronal release of MAPT/tau variants, thus contributing to MAPT/tau propagation.
“Blockage of CMA leads to rerouting of some of the pathogenic forms of MAPT/tau toward endosomal microautophagy, as both pathways share the same chaperone, HSPA8, and this promotes fusion of late endosomes with the plasma membrane and subsequent extraneuronal release of the MAPT/tau variants, thus contributing to MAPT/tau propagation (Caballero et al, 2021).”
From Autophagy in major human diseases (2021) · cites this paper as Caballero et al, 2021
Mutations and posttranslational modifications of MAPT/tau, such as acetylation, not only prevent MAPT/tau degradation by CMA but also inhibit normal CMA functioning.
“However, mutations and posttranslational modifications of this protein, such as acetylation, not only prevent MAPT/tau degradation by CMA but also inhibit normal CMA functioning (Caballero et al, 2018; Caballero et al, 2021).”
From Autophagy in major human diseases (2021) · cites this paper as Caballero et al, 2021
Chaperone-mediated autophagy contributes to degradation of a large fraction of neuronal MAPT/tau under physiological conditions.
“Chaperone‐mediated autophagy also contributes to degradation of a large fraction of neuronal MAPT/tau under physiological conditions (Caballero et al, 2018; Caballero et al, 2021).”
From Autophagy in major human diseases (2021) · cites this paper as Caballero et al, 2021
Reduction in neuronal CMA activity has been shown in AD patient's brains.
“Reduction in neuronal CMA activity has been recently shown in AD patient's brains (Bourdenx et al, 2021; Caballero et al, 2021)”
From Autophagy in major human diseases (2021) · cites this paper as Caballero et al, 2021
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- Authors
- Caballero, B., Bourdenx, M., Luengo, E., Diaz, A., Sohn, P. D., Chen, X., Wang, C., Juste, Y. R., Wegmann, S., Patel, B., Young, Z. T., Kuo, S. Y., Rodriguez-Navarro, J. A., Shao, H., Lopez, M. G., Karch, C. M., Goate, A. M., Gestwicki, J. E., Hyman, B. T., Gan, L., & Cuervo, A. M.
- Affiliations
- Albert Einstein College of Medicine (US)
- Centre National de la Recherche Scientifique (FR)
- Weill Cornell Medicine (US)
- Harvard University (US)
- University of California, San Francisco (US)
- Washington University in St. Louis (US)
- Icahn School of Medicine at Mount Sinai (US)
- ORCID
- Venue
- Nature Communications
- Published
- 2021-04-14
- Volume
- 12
- Issue
- 1
- Pages
- 2238-2238
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC8047017
- OpenAlex
- W3154991192
- Cited by
- 223
- References
- 92
- Citations by year
- 2026: 29 · 2025: 61 · 2024: 30 · 2023: 47 · 2022: 42 · 2021: 14
- FWCI
- 20.89
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Digital Commons@Becker (Washington University School of Medicine) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- eScholarship (California Digital Library) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- DZNE Pub (submittedVersion, other-oa)
- Funders
- Fundación Tatiana Pérez de Guzmán el Bueno (Fellowship)
- U.S. Department of Health & Human Services | National Institutes of Health (T32 GM007491)
- Charles H. Revson Foundation (CP13-00234)
- Rainwaters Foundation
- U.S. Department of Health & Human Services | NIH | National Institute on Aging (AG05681, AG058674, AG036884, AG021904, AG054108, AG031782, AG038072)
- Rainwaters Foundation JPB Foundation
- U.S. Department of Health & Human Services | NIH | National Institute of Neurological Disorders and Stroke (NS100717)
- Rainwaters Foundation Backus Foundation JPB Foundation
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- tau acetylation, chaperone-mediated autophagy, tauopathy, tau degradation, macroautophagy, microautophagy, lysosomes, cell-to-cell transmission, neurodegeneration
- MeSH terms
- Chaperone-Mediated Autophagy, Acetylation, Animals, Brain, Female, Humans, Male, Mice, Inbred C57BL, Neurons, tau Proteins, Tauopathies, Mice
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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