Evidence map›Paper›PMID 34621743›Full record

ReviewFrontiers in cell and developmental biology2021

Tau and Membranes: Interactions That Promote Folding and Condensation.

Chad A Sallaberry, Barbie J Voss, Jaroslaw Majewski, Jacek Biernat, Eckhard Mandelkow, Eva Y Chi, Crystal M Vander Zanden

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in cell and developmental biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

31 citing papers in PubMed, 59 citations in OpenAlex.

  1. Differential proteostasis imbalance and the molecular basis of distinct synucleinopathies and tauopathies.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
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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

7 authors at 5 institutions in 2 countries.

Chad A SallaberryDepartment of Chemistry & Biochemistry, University of Colorado Colorado Springs, Colorado Springs, CO, United States.
Barbie J VossDepartment of Chemistry & Biochemistry, University of Colorado Colorado Springs, Colorado Springs, CO, United States.
Jaroslaw MajewskiDivision of Molecular and Cellular Biosciences, National Science Foundation, Alexandria, VA, United States.
Jacek BiernatGerman Center for Neurodegenerative Diseases (DZNE), Bonn, Germany.
Eckhard MandelkowGerman Center for Neurodegenerative Diseases (DZNE), Bonn, Germany.
Eva Y ChiDepartment of Chemical & Biological Engineering, Center for Biomedical Engineering, The University of New Mexico, Albuquerque, NM, United States.
Crystal M Vander ZandenDepartment of Chemistry & Biochemistry, University of Colorado Colorado Springs, Colorado Springs, CO, United States.
University of Colorado Colorado Springs · USGerman Center for Neurodegenerative Diseases · DELos Alamos National Laboratory · USUniversity of Bonn · DEUniversity of New Mexico · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tau misfolding and assembly is linked to a number of neurodegenerative diseases collectively described as tauopathies, including Alzheimer's disease (AD) and Parkinson's disease. Anionic cellular membranes, such as the cytosolic leaflet of the plasma membrane, are sites that concentrate and neutralize tau, primarily due to electrostatic interactions with tau's microtubule binding repeat domain (RD). In addition to electrostatic interactions with lipids, tau also has interactions with membrane proteins, which are important for tau's cellular functions. Tau also interacts with lipid tails to facilitate direct translocation across the membrane and can form stable protein-lipid complexes involved in cell-to-cell transport. Concentrated tau monomers at the membrane surface can form reversible condensates, change secondary structures, and induce oligomers, which may eventually undergo irreversible crosslinking and fibril formation. These β-sheet rich tau structures are capable of disrupting membrane organization and are toxic in cell-based assays. Given the evidence for relevant membrane-based tau assembly, we review the emerging hypothesis that polyanionic membranes may serve as a site for phase-separated tau condensation. Membrane-mediated phase separation may have important implications for regulating tau folding/misfolding, and may be a powerful mechanism to spatially direct tau for native membrane-mediated functions.

Indexed as

condensationfibrilsintrinsically disordered proteinmembranephase separationpolyanionic surfacetau

Identifiers

PMID34621743
PMCPMC8491580
OpenAlexW3200042857

What OpenQuestion holds

Textmetadata
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.