Evidence map›Paper›PMID 31667556›Full record

ReviewCellular and molecular life sciences : CMLS2020

Mechanisms of secretion and spreading of pathological tau protein.

Cecilia A Brunello, Maria Merezhko, Riikka-Liisa Uronen, Henri J Huttunen

Open access · hybridAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 174 papers.

0numbers the graph read from it
0cells of the map it votes in
174citing papers in PubMed
18.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

174 citing papers in PubMed, 302 citations in OpenAlex.

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  11. Frontotemporal dementia associated CHCHD10Cell death & disease · 2026
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114 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Cecilia A BrunelloNeuroscience Center, HiLIFE, University of Helsinki, P.O. Box 63, Haartmaninkatu 8, 00014, Helsinki, Finland.
Maria MerezhkoNeuroscience Center, HiLIFE, University of Helsinki, P.O. Box 63, Haartmaninkatu 8, 00014, Helsinki, Finland.
Riikka-Liisa UronenNeuroscience Center, HiLIFE, University of Helsinki, P.O. Box 63, Haartmaninkatu 8, 00014, Helsinki, Finland.
Henri J HuttunenNeuroscience Center, HiLIFE, University of Helsinki, P.O. Box 63, Haartmaninkatu 8, 00014, Helsinki, Finland. henri.huttunen@helsinki.fi.ORCID http://orcid.org/0000-0002-9867-4438
University of Helsinki · FI

Funding

Academy of Finland 296409
6 · The paper itself

Abstract

Accumulation of misfolded and aggregated forms of tau protein in the brain is a neuropathological hallmark of tauopathies, such as Alzheimer's disease and frontotemporal lobar degeneration. Tau aggregates have the ability to transfer from one cell to another and to induce templated misfolding and aggregation of healthy tau molecules in previously healthy cells, thereby propagating tau pathology across different brain areas in a prion-like manner. The molecular mechanisms involved in cell-to-cell transfer of tau aggregates are diverse, not mutually exclusive and only partially understood. Intracellular accumulation of misfolded tau induces several mechanisms that aim to reduce the cellular burden of aggregated proteins and also promote secretion of tau aggregates. However, tau may also be released from cells physiologically unrelated to protein aggregation. Tau secretion involves multiple vesicular and non-vesicle-mediated pathways, including secretion directly through the plasma membrane. Consequently, extracellular tau can be found in various forms, both as a free protein and in vesicles, such as exosomes and ectosomes. Once in the extracellular space, tau aggregates can be internalized by neighboring cells, both neurons and glial cells, via endocytic, pinocytic and phagocytic mechanisms. Importantly, accumulating evidence suggests that prion-like propagation of misfolding protein pathology could provide a general mechanism for disease progression in tauopathies and other related neurodegenerative diseases. Here, we review the recent literature on cellular mechanisms involved in cell-to-cell transfer of tau, with a particular focus in tau secretion.

Indexed as

AnimalsDisease ProgressionHumansProtein Aggregation, PathologicalTauopathiestau Proteinstau ProteinsAggregationAmyloidExtracellular vesiclesPrionPropagationTauUnconventional protein secretion

Identifiers

PMID31667556
PMCPMC7190606
OpenAlexW2982627322

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.