Evidence map›Paper›PMID 29215007›Full record

ArticleNature communications2017

Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau.

Yunior Cabrales Fontela, Harindranath Kadavath, Jacek Biernat, Dietmar Riedel, Eckhard Mandelkow, Markus Zweckstetter

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

77 citing papers in PubMed, 156 citations in OpenAlex.

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  13. cUMP elicits interendothelial gap formation duringAmerican journal of physiology. Lung cellular and molecular physiology · 2024
    Article
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  15. Cell autonomous microglia defects in a stem cell model of frontotemporal dementia.medRxiv : the preprint server for health sciences · 2024
    Article
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17 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

6 authors at 3 institutions in 1 country.

Yunior Cabrales FontelaDeutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Von-Siebold-Strasse 3a, 37075, Göttingen, Germany.
Harindranath KadavathDeutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Von-Siebold-Strasse 3a, 37075, Göttingen, Germany.
Jacek BiernatDeutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Ludwig-Erhard-Allee 2, 53175, Bonn, Germany.
Dietmar RiedelMax-Planck-Institut für Biophysikalische Chemie, Am Faßberg 11, 37077, Göttingen, Germany.
Eckhard MandelkowDeutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Ludwig-Erhard-Allee 2, 53175, Bonn, Germany.
Markus ZweckstetterDeutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Von-Siebold-Strasse 3a, 37075, Göttingen, Germany. Markus.Zweckstetter@dzne.de.ORCID http://orcid.org/0000-0002-2536-6581
German Center for Neurodegenerative Diseases · DECenter of Advanced European Studies and Research · DEMax Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubule-associated proteins regulate microtubule dynamics, bundle actin filaments, and cross-link actin filaments with microtubules. In addition, aberrant interaction of the microtubule-associated protein Tau with filamentous actin is connected to synaptic impairment in Alzheimer's disease. Here we provide insight into the nature of interaction between Tau and actin filaments. We show that Tau uses several short helical segments to bind in a dynamic, multivalent process to the hydrophobic pocket between subdomains 1 and 3 of actin. Although a single Tau helix is sufficient to bind to filamentous actin, at least two, flexibly linked helices are required for actin bundling. In agreement with a structural model of Tau repeat sequences in complex with actin filaments, phosphorylation at serine 262 attenuates binding of Tau to filamentous actin. Taken together the data demonstrate that bundling of filamentous actin and cross-linking of the cellular cytoskeleton depend on the metamorphic and multivalent nature of microtubule-associated proteins.

Indexed as

Actin CytoskeletonActin Depolymerizing FactorsAlzheimer DiseaseHumansHydrophobic and Hydrophilic InteractionsMicrotubule-Associated ProteinsMicrotubulesMolecular Docking SimulationPhosphorylationProtein Interaction Domains and MotifsSerinetau ProteinsActin Depolymerizing FactorsMicrotubule-Associated ProteinsSerinetau Proteins

Identifiers

PMID29215007
PMCPMC5719408
OpenAlexW2771232440

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.