Evidence map›Paper›PMID 40064283›Full record

ArticleProgress in neurobiology2025

Pathogenic oligomeric Tau alters neuronal RNA processes through the formation of nuclear heteromeric amyloids with RNA-binding protein Musashi1.

Nicha Puangmalai, Abbigael E Aday, Madison Samples, Nemil Bhatt, Filippa Lo Cascio, Michela Marcatti, Suhyeorn J Park, Leiana Fung, Cynthia Jerez, Luiz O Penalva and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Progress in neurobiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

15 authors.

Nicha PuangmalaiMitchell Center for Neurodegenerative Diseases, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA; Departments of Neurology, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: nipuangm@utmb.edu.
Abbigael E AdayMitchell Center for Neurodegenerative Diseases, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA; Departments of Neurology, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: aeaday@utmb.edu.
Madison SamplesMitchell Center for Neurodegenerative Diseases, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA; Departments of Neurology, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: masample@utmb.edu.
Nemil BhattMitchell Center for Neurodegenerative Diseases, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA; Departments of Neurology, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: nebhatt@utmb.edu.
Filippa Lo CascioMitchell Center for Neurodegenerative Diseases, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA; Departments of Neurology, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: filippalocascio@gmail.com.
Michela MarcattiMitchell Center for Neurodegenerative Diseases, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA; Departments of Neurology, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: mimarcat@utmb.edu.
Suhyeorn J ParkMitchell Center for Neurodegenerative Diseases, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA; Departments of Neurology, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: sujpark@utmb.edu.
Leiana FungMitchell Center for Neurodegenerative Diseases, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA; Departments of Neurology, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: leiana.fung@gmail.com.
Cynthia JerezMitchell Center for Neurodegenerative Diseases, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA; Departments of Neurology, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: cyjerez@utmb.edu.
Luiz O PenalvaGreehey Children's Cancer Research Institute, The University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr, San Antonio, TX 78229, USA; Department of Cell Systems and Anatomy, The University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr, San Antonio, TX 78229, USA. Electronic address: penalva@uthscsa.edu.
Yingxin ZhaoDepartment of Internal Medicine, The University of Texas Medical Branch, 301 University Blvd, Galveston TX 77555, USA. Electronic address: yizhao@utmb.edu.
Haiping HaoDirector, UTMB Next Gen Sequencing Core, Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, 301 University Blvd., Galveston, TX 77555, USA. Electronic address: hahao@utmb.edu.
Doreen LuganoKEMRI-Wellcome Trust Research Programme, P.O. Box 230, Kilifi Kenya. Electronic address: dlugano@kemri-wellcome.org.
Rakez KayedMitchell Center for Neurodegenerative Diseases, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA; Departments of Neurology, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: rakayed@utmb.edu.
Mauro MontalbanoMitchell Center for Neurodegenerative Diseases, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA; Departments of Neurology, The University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: mamontal@utmb.edu.

Funding

Interdisciplinary Research Network on Biologically Active Tau Aggregate Polymorphs from Alzheimer's Disease and Related DementiasU24AG072458 · NIA · UNIVERSITY OF TEXAS MED BR GALVESTON · PI EISENBERG, DAVID, KAYED, RAKEZ · 2021 to 2025
$7.8M
Formation and Propagation of Tau Oligomeric Strains in Alzheimer's DiseaseR01AG054025 · NIA · UNIVERSITY OF TEXAS MED BR GALVESTON · PI Rakez Kayed · 2016 to 2026
$5.8M
The Role of Ubiquitination in Tau Oligomers PathogenesisR01AG077253 · NIA · UNIVERSITY OF TEXAS MED BR GALVESTON · PI Rakez Kayed, Yingxin Zhao · 2022 to 2026
$3.7M
Calcineurin Mediates the Synergistic Toxicity of Tau and Aβ OligomersRF1AG060718 · NIA · UNIVERSITY OF TEXAS MED BR GALVESTON · PI KAYED, RAKEZ, TAGLIALATELA, GIULIO · 2019 to 2019
$3.5M
Tau in the Eye and BrainRF1AG055771 · NIA · UNIVERSITY OF TEXAS MED BR GALVESTON · PI KAYED, RAKEZ, ZHANG, WENBO · 2017 to 2017
$2.7M
Immunotherapy Targeting Tau Aggregate PolymorphsRF1AG077484 · NIA · UNIVERSITY OF TEXAS MED BR GALVESTON · PI KAYED, RAKEZ · 2022 to 2022
$2.0M
Musashi1 and miR-137 antagonism: impact on neurogenesis and diseasesR21NS113344 · NINDS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI KOKOVAY, ERZSEBET, PENALVA, LUIZ OTAVIO · 2020 to 2020
$425k
Calcineurin Mediates the Synergistic Toxicity of Tau and Aβ OligomersR01AG060718 · NIA · UNIVERSITY OF TEXAS MED BR GALVESTON · PI KAYED, RAKEZ, TAGLIALATELA, GIULIO · 2019 to 2019
$39k
NIA NIH HHS R01 AG054025NIA NIH HHS R01 AG060718NIA NIH HHS R01 AG077253NIA NIH HHS RF1 AG055771NIA NIH HHS RF1 AG060718NIA NIH HHS RF1 AG077484NIA NIH HHS U24 AG072458NINDS NIH HHS R21 NS113344
6 · The paper itself

Abstract

Alzheimer's disease (AD) is marked by cytoplasmic proteinopathies, primarily involving misfolded Tau protein. Pathogenic Tau species, such as soluble oligomers and fibrils, disrupt RNA metabolism, though the mechanisms are unclear. Recent research indicates that RNA has a crucial role in Tau aggregation. Our study builds on this by noting significant co-deposition of RNA-Binding Proteins (RBPs) with Tau in AD and Frontotemporal dementia (FTLD) brains. Using molecular and cellular techniques, we investigate the interaction between RNA dynamics and Tau aggregation, focusing on the localization and aggregation of Tau and RBPs, particularly Musashi (MSI), within neuronal nuclei. Through cyto-fluorometric, biochemical, and cellular assays, we reveal the importance of Tau/RBP interplay in primary cortical neurons expressing wild-type and mutant Tau. Pathogenic Tau oligomers alter MSI protein localization and function, causing cytoplasmic and nuclear aggregation. Mass spectrometry of the MSI1 nuclear interactome in Tau models shows disrupted RNA metabolism pathways, including ribosomal biogenesis, RNA splicing, and protein folding. Moreover, RNA immunoprecipitation assay revealed a remarkable impact of mutant P301L Tau on MSI1 ability to bind RNA targets. These findings highlight potential targets for early neurodegenerative therapeutic interventions.

Indexed as

AmyloidNerve Tissue ProteinsNeuronsRNARNA-Binding Proteinstau ProteinsAnimalsCell NucleusCells, CulturedHumansMiceAmyloidMSI1 protein, humanNerve Tissue ProteinsRNARNA-Binding Proteinstau ProteinsAggregationMusashiNucleusRNA processingTau

Identifiers

PMID40064283
PMCPMC11984483

What OpenQuestion holds

Textmetadata
LicenceTDM
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.