LRP1 is a master regulator of tau uptake and spread
Open accessAbstract
The spread of protein aggregates during disease progression is a common theme underlying many neurodegenerative diseases. The microtubule-associated protein tau has a central role in the pathogenesis of several forms of dementia known as tauopathies-including Alzheimer's disease, frontotemporal dementia and chronic traumatic encephalopathy 1. Progression of these diseases is characterized by the sequential spread and deposition of protein aggregates in a predictable pattern that correlates with clinical severity 2. This observation and complementary experimental studies 3,4 have suggested that tau can spread in a prion-like manner, by passing to naive cells in which it templates misfolding and aggregation. However, although the propagation of tau has been extensively studied, the underlying cellular mechanisms remain poorly understood. Here we show that the low-density lipoprotein receptor-related protein 1 (LRP1) controls the endocytosis of tau and its subsequent spread. Knockdown of LRP1 significantly reduced tau uptake in H4 neuroglioma cells and in induced pluripotent stem cell-derived neurons. The interaction between tau and LRP1 is mediated by lysine residues in the microtubule-binding repeat region of tau. Furthermore, downregulation of LRP1 in an in vivo mouse model of tau spread was found to effectively reduce the propagation of tau between neurons. Our results identify LRP1 as a key regulator of tau spread in the brain, and therefore a potential target for the treatment of diseases that involve tau spread and aggregation.
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APOE binding is integral to some processes involving lipoprotein receptors, including Aβ aggregation and neuronal uptake of extracellular tau.
“Studies indicate that APOE binding is integral to some of these processes [16–20] with differences in APOE isoform-specific receptor binding affinity and lipid interactions affecting neuroinflammation, tau pathology, and amyloid plaque dynamics [21–24].”
From APOE Christchurch enhances a disease-associated microglial response to plaque but suppresses response to tau pathology (2025) · cites this paper as [20]
The Results (page not available) report that ApoE-containing medium reduced extracellular tau uptake in H4 neuroglioma cells and that LRP1 regulates tau uptake in neurons. They also discuss ApoE4-dependent Aβ pathology, but do not establish an effect on Aβ aggregation or test ApoE’s effect on tau uptake specifically in neurons. (LLM, conf=0.85)
Experimental — accuracy not yet measuredAPOE and APOE3Ch influence both Aβ and tau pathology, either directly or through downstream effects such as neuroinflammation.
“Collectively, these recent findings underscore the influence of APOE and APOE3Ch on both Aβ and tau pathology, either directly or through downstream effects such as neuroinflammation.”
From APOE Christchurch enhances a disease-associated microglial response to plaque but suppresses response to tau pathology (2025) · cites this paper as [20]
The Results (page not supplied) state that ApoE4 has been shown to exacerbate Aβ pathology and worsen tau pathology, and report that ApoE-containing medium reduced tau uptake. The copy does not address APOE3Ch or identify neuroinflammation as a downstream mechanism for these effects. (LLM, conf=0.88)
Experimental — accuracy not yet measuredMammalian expression systems retain physiologically relevant secretory, folding and post-translational modification mechanisms.
“Mammalian expression systems retain physiologically relevant secretory, folding and post-translational modification mechanisms, but column-purified recombinant ApoE is invariably prepared as apoprotein.22–25”
From ApoE is Secreted as a Lipid Nanoparticle by Mammalian Cells: Implications for Alzheimer’s Disease Pathogenesis (2025) · cites this paper as [24]
The Methods (Cell Culture; page unavailable) report that HEK293T cells expressed ApoE and that ApoE was detected in their conditioned medium, supporting secretion from a mammalian expression system. The paper does not establish that such systems retain physiologically relevant folding or post-translational modification mechanisms. (LLM, conf=0.78)
Experimental — accuracy not yet measuredApoE in general reduces LRP1-mediated tau uptake by neurons and propagation.
“it has been observed that ApoE in general reduces LRP1-mediated tau uptake by neurons and propagation [52]”
From Apoe4 and Alzheimer’s Disease Pathogenesis—Mitochondrial Deregulation and Targeted Therapeutic Strategies (2023) · cites this paper as [52]
The Results report that ApoE-conditioned medium significantly reduced full-length tau uptake in H4 cells, and suggest that ApoE could inhibit tau–LRP1 interactions and suppress tau spread. The ApoE uptake experiment was not performed in neurons, and the paper does not report a direct test of ApoE's effect on tau propagation; those parts of the claim overstate the evidence. (LLM, conf=0.88)
Experimental — accuracy not yet measuredLRP1 has been shown to mediate tau uptake in vitro and drastically increase the propagation of the P301L human tau protein expressed by an AAV virus in vivo.
“The other primary apoE metabolic receptor, LRP1, has been shown to mediate tau uptake in vitro and drastically increase the propagation of the P301L human tau protein expressed by an AAV virus in vivo (Rauch et al., 2020)”
From Overexpressing low‐density lipoprotein receptor reduces tau‐associated neurodegeneration in relation to apoE‐linked mechanisms (2021) · cites this paper as Rauch et al., 2020
LRP1 mediates tau endocytosis and promotes tau propagation between neurons.
“LRP1 mediates tau endocytosis and promotes tau propagation between neurons”
From ApoE4 reduction: An emerging and promising therapeutic strategy for Alzheimer's disease (2022) · cites this paper as Rauch et al 2020
LRP1 mediates tau uptake by neurons and is involved in tau spreading.
“LRP1 also mediates tau uptake by neurons, being involved in tau spreading.”
From Apoe4 and Alzheimer’s Disease Pathogenesis—Mitochondrial Deregulation and Targeted Therapeutic Strategies (2023) · cites this paper as [52]
Decreased total ApoE levels are possibly related to potentiation of tau pathology through enhanced LRP-1 mediated tau propagation.
“which is possibly related to the potentiation of tau pathology throw enhanced LRP-1 mediated tau propagation [52]”
From Apoe4 and Alzheimer’s Disease Pathogenesis—Mitochondrial Deregulation and Targeted Therapeutic Strategies (2023) · cites this paper as [52]
Column-purified recombinant ApoE is invariably prepared as apoprotein.
“Mammalian expression systems retain physiologically relevant secretory, folding and post-translational modification mechanisms, but column-purified recombinant ApoE is invariably prepared as apoprotein.22–25”
From ApoE is Secreted as a Lipid Nanoparticle by Mammalian Cells: Implications for Alzheimer’s Disease Pathogenesis (2025) · cites this paper as [24]
The Methods (Cell Culture) and Results describe ApoE expressed in HEK293T cells and used in conditioned medium, not column-purified ApoE. The Methods (Protein Purification and Labeling) describe column purification of other proteins but do not say whether column-purified recombinant ApoE is invariably an apoprotein. Searches for ApoE apoprotein, lipidation, and column purification found no passage addressing that claim. (LLM, conf=0.76)
Experimental — accuracy not yet measuredApoE is not detected in appreciable quantities in its apo form in physiological fluids.
“Although ApoE is not detected in appreciable quantities in its apo form in physiological fluids, to date all reports describing the biochemical properties of this recombinant protein have deployed lipid-free biosynthetic materials.21–25”
From ApoE is Secreted as a Lipid Nanoparticle by Mammalian Cells: Implications for Alzheimer’s Disease Pathogenesis (2025) · cites this paper as [24]
The Results and Cell Culture Methods describe ApoE in conditioned medium and its effect on tau uptake, but do not address whether appreciable quantities of lipid-free ApoE occur in physiological fluids. Searches for ApoE’s apo form, lipidation, and physiological fluids found no passage supporting that claim. The copy also does not assess whether prior biochemical reports used lipid-free recombinant ApoE. (LLM, conf=0.74)
Experimental — accuracy not yet measuredTo date all reports describing the biochemical properties of this recombinant protein have deployed lipid-free biosynthetic materials.
“Although ApoE is not detected in appreciable quantities in its apo form in physiological fluids, to date all reports describing the biochemical properties of this recombinant protein have deployed lipid-free biosynthetic materials.21–25”
From ApoE is Secreted as a Lipid Nanoparticle by Mammalian Cells: Implications for Alzheimer’s Disease Pathogenesis (2025) · cites this paper as [24]
The Methods (Cell Culture) describe producing ApoE in HEK293T cells and collecting conditioned medium, while the Results examine its effect on tau uptake. Neither section addresses whether the ApoE was lipid-free or whether all prior biochemical reports used lipid-free recombinant material (searched: lipid-free ApoE, lipidated ApoE). (LLM, conf=0.74)
Experimental — accuracy not yet measuredSuch screens yield rich information about processes including differentiation, immune responses, stress responses and compensatory responses, and allow high-throughput mapping of regulatory elements.
“Such screens provide rich information on cellular processes such as differentiation72, immune responses72,73,75, stress responses74 and compensatory responses76 and enable high-throughput mapping of regulatory elements77.”
From CRISPR-based functional genomics for neurological disease (2020) · cites this paper as [72]
Pooled CRISPR screens can be combined with single-cell RNA sequencing to give high-dimensional readouts of gene perturbation effects.
“While screens based on survival or FACS monitor low-dimensional phenotypes, pooled CRISPR screens can also be coupled to single-cell RNA sequencing to provide high-dimensional readouts of the effects of gene perturbation72–75”
From CRISPR-based functional genomics for neurological disease (2020) · cites this paper as [72]
LRP1 expressed in neurons regulates the endocytosis of tau and its subsequent spread.
“A recent study showed that the low-density lipoprotein receptor-related protein 1 (LRP1) expressed in neurons regulates the endocytosis of tau and its subsequent spread [74].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [74]
Knockdown or inhibition of LRP1 significantly reduces tau uptake and spread in vitro and in vivo.
“Knockdown or inhibition of LRP1 significantly reduces tau uptake and spread in vitro and in vivo [74].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [74]
LRP1 appears to be a primary mechanism subverting uptake of soluble extracellular tau, allowing it to escape degradation and be released to cytoplasm.
“For example, the multifunctional receptor LRP1 appears to be a primary mechanism subverting uptake of soluble extracellular tau (58, 59), so that it can at least partly escape degradation and be released to the cytoplasm.”
From All the Tau We Cannot See (2023) · cites this paper as [59]
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“A recent study showed that the low-density lipoprotein receptorrelated protein 1 (LRP1) expressed in neurons regulates the endocytosis of tau and its subsequent spread [74].”
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- Authors
- Rauch, J. N., Luna, G., Guzman, E., Audouard, M., Challis, C., Sibih, Y. E., Leshuk, C., Hernandez, I., Wegmann, S., Hyman, B. T., Gradinaru, V., Kampmann, M., & Kosik, K. S.
- Affiliations
- University of California, Santa Barbara (US)
- California Institute of Technology (US)
- German Center for Neurodegenerative Diseases (DE)
- Harvard University (US)
- QB3 (US)
- Corresponding author
- Kosik, Kenneth S.
- ORCID
- Venue
- Nature
- Published
- 2020-04-01
- Volume
- 580
- Issue
- 7803
- Pages
- 381-385
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC7687380
- OpenAlex
- W3014222043
- Cited by
- 541
- References
- 34
- Citations by year
- 2026: 58 · 2025: 85 · 2024: 93 · 2023: 90 · 2022: 73 · 2021: 85 · 2020: 57
- FWCI
- 45.85
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DZNE Pub (submittedVersion)
- Funders
- Larry L. Hillblom Foundation
- Dr. Miriam and Sheldon G. Adelson Medical Research Foundation
- Edward N. and Della L. Thome Memorial Foundation
- Deutsches Zentrum für Neurodegenerative Erkrankungen
- National Institutes of Health (1r56ag057528-01a1)
- University of California, Santa Barbara
- National Institute on Aging (R56AG062479, R01AG023100, R56 AG057528, RF1AG059789, K99AG064116, R01AG062359, P30AG062421)
- National Institute of General Medical Sciences (DP2GM119139)
- National Institute of Neurological Disorders and Stroke (U54NS100717)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- LRP1, tau protein, tau spread, tauopathy, Alzheimer's disease, frontotemporal dementia, chronic traumatic encephalopathy, prion-like propagation, endocytosis, lysine residues, microtubule-binding repeats, neurodegeneration, iPSC-derived neurons
- MeSH terms
- Animals, Cell Line, Endocytosis, Female, Humans, Ligands, Male, Neurons, tau Proteins, Low Density Lipoprotein Receptor-Related Protein-1, Mice
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