Evidence map›Paper›PMID 35567706›Full record

ArticleMolecular neurobiology2022

SUMO1 Modification of Tau in Progressive Supranuclear Palsy.

Hironori Takamura, Yoshiaki Nakayama, Hidefumi Ito, Taiichi Katayama, Paul E Fraser, Shinsuke Matsuzaki

Open access · hybridAbstract read
In one paragraph

Article in Molecular neurobiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Characterization of Isolated Human Astrocytes from Aging Brain.International journal of molecular sciences · 2025
    Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Review
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 4 institutions in 3 countries.

Hironori TakamuraTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, ON, Canada.
Yoshiaki NakayamaDepartment of Neurology, Wakayama Medical University, Wakayama, Japan.
Hidefumi ItoDepartment of Neurology, Wakayama Medical University, Wakayama, Japan.
Taiichi KatayamaDepartment of Child Development & Molecular Brain Science, Center for Child Mental Development, United Graduate School of Child Development, Osaka University, Osaka, Japan.
Paul E FraserTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, ON, Canada.
Shinsuke MatsuzakiDepartment of Child Development & Molecular Brain Science, Center for Child Mental Development, United Graduate School of Child Development, Osaka University, Osaka, Japan. shinsuke_matsuzaki@morinomiya-u.ac.jp.ORCID http://orcid.org/0000-0003-1786-7148
University of Toronto · CAWakayama Medical University · JPMorinomiya University of Medical Sciences · JPNational Center For Child Health and Development · JP

Funding

Canadian Institute of Health Research PJT-173497Canadian Institute of Health Research TAD-117950Japanese Society for the Promotion of Science 17KK0197Japan Society for the Promotion of Science 18H02743Japan Society for the Promotion of Science 26860133Japan Society for the Promotion of Science S2603
6 · The paper itself

Abstract

Small ubiquitin-like modifiers (SUMO) have been implicated in several neurodegenerative diseases. SUMO1 conjugation has been shown to promote aggregation and regulate phosphorylation of the tau protein linked to Alzheimer's disease and related tauopathies. The current study has demonstrated that SUMO1 co-localizes with intraneuronal tau inclusions in progressive supranuclear palsy (PSP). Immunoprecipitation of isolated and solubilized tau fibrils from PSP tissues revealed SUMO1 conjugation to a cleaved and N-terminally truncated tau. The effects of SUMOylation were examined using tau-SUMO fusion proteins which showed a higher propensity for tau oligomerization of PSP-truncated tau and accumulation on microtubules as compared to the full-length protein. This was found to be specific for SUMO1 as the corresponding SUMO2 fusion protein did not display a significantly altered cytoplasmic distribution or aggregation of tau. Blocking proteasome-mediated degradation promoted the aggregation of the tau fusion proteins with the greatest effect observed for truncated tau-SUMO1. The SUMO1 modification of the truncated tau in PSP may represent a detrimental event that promotes aggregation and impedes the ability of cells to remove the resulting protein deposits. This combination of tau truncation and SUMO1 modification may be a contributing factor in PSP pathogenesis.

Indexed as

Alzheimer DiseaseSupranuclear Palsy, ProgressiveTauopathiesHumansNeurofibrillary TanglesSUMO-1 Proteintau ProteinsUbiquitinsSUMO-1 ProteinSUMO1 protein, humantau ProteinsUbiquitinsNeurodegenerationNeurofibrillary tanglesProtein aggregationSmall ubiquitin-like modifiers (SUMO)TauopathyTruncated tau

Identifiers

PMID35567706
PMCPMC9167224
OpenAlexW4280641207

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.