Evidence map›Paper›PMID 31700063›Full record

ArticleScientific reports2019

Tau interactome analyses in CRISPR-Cas9 engineered neuronal cells reveal ATPase-dependent binding of wild-type but not P301L Tau to non-muscle myosins.

Xinzhu Wang, Declan Williams, Iris Müller, Mackenzie Lemieux, Ramona Dukart, Isabella B L Maia, Hansen Wang, Amanda L Woerman, Gerold Schmitt-Ulms

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Modified tau leads to neuronal and global ribosome dysfunction inbioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. TauCell death & disease · 2024
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Background and roles: myosin in autoimmune diseases.Frontiers in cell and developmental biology · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
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

9 authors at 2 institutions in 2 countries.

Xinzhu WangTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Ontario, M5T 2S8, Canada.ORCID http://orcid.org/0000-0002-1438-1153
Declan WilliamsTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Ontario, M5T 2S8, Canada.
Iris MüllerTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Ontario, M5T 2S8, Canada.
Mackenzie LemieuxTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Ontario, M5T 2S8, Canada.ORCID http://orcid.org/0000-0001-6015-8668
Ramona DukartDepartment of Laboratory Medicine & Pathobiology, University of Toronto, Ontario, M5S 1A8, Canada.
Isabella B L MaiaTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Ontario, M5T 2S8, Canada.
Hansen WangTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Ontario, M5T 2S8, Canada.
Amanda L WoermanDepartment of Neurology, University of California San Francisco, California, 94158, USA.
Gerold Schmitt-UlmsTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Ontario, M5T 2S8, Canada. g.schmittulms@utoronto.ca.ORCID http://orcid.org/0000-0001-6962-0919
University of Toronto · CAUniversity of California, San Francisco · US

Funding

CIHR 137651
6 · The paper itself

Abstract

Protein interactions of Tau are of interest in efforts to decipher pathogenesis in Alzheimer's disease, a subset of frontotemporal dementias, and other tauopathies. We CRISPR-Cas9 edited two human cell lines to generate broadly adaptable models for neurodegeneration research. We applied the system to inducibly express balanced levels of 3-repeat and 4-repeat wild-type or P301L mutant Tau. Following 12-h induction, quantitative mass spectrometry revealed the Parkinson's disease-causing protein DJ-1 and non-muscle myosins as Tau interactors whose binding to Tau was profoundly influenced by the presence or absence of the P301L mutation. The presence of wild-type Tau stabilized non-muscle myosins at higher steady-state levels. Strikingly, in human differentiated co-cultures of neuronal and glial cells, the preferential interaction of non-muscle myosins to wild-type Tau depended on myosin ATPase activity. Consistently, transgenic P301L Tau mice exhibited reduced phosphorylation of regulatory myosin light chains known to activate this ATPase. The direct link of Tau to non-muscle myosins corroborates independently proposed roles of Tau in maintaining dendritic spines and mitochondrial fission biology, two subcellular niches affected early in tauopathies.

Indexed as

Cell EngineeringMutationProtein Interaction MappingAdenosine TriphosphatasesAstrocytesCoculture TechniquesCRISPR-Cas SystemsHumansMyosinsNeuronsProtein Bindingtau ProteinsAdenosine TriphosphatasesMyosinstau Proteins

Identifiers

PMID31700063
PMCPMC6838314
OpenAlexW2984978709

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.