Evidence map›Paper›PMID 32393629›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

TDP-43 dysfunction restricts dendritic complexity by inhibiting CREB activation and altering gene expression.

Josiah J Herzog, Weijin Xu, Mugdha Deshpande, Reazur Rahman, Hannah Suib, Avital A Rodal, Michael Rosbash, Suzanne Paradis

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed, 1 pooled it
3.0field-weighted citation impact, top 7% 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

33 citing papers in PubMed, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Early disruption of the CREB pathway drives dendritic morphological alterations in FTD/ALS cortical neurons.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. cAMP/PKA signaling regulates TDP-43 aggregation and mislocalization.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Review
  11. Article
  12. Identification of RNA-Binding Protein Targets with HyperTRIBE inInternational journal of molecular sciences · 2023
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Review
  19. Review
  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

8 authors at 2 institutions in 1 country.

Josiah J HerzogDepartment of Biology, Brandeis University, Waltham, MA 02453.
Weijin XuDepartment of Biology, Brandeis University, Waltham, MA 02453.ORCID 0000-0003-1634-5241
Mugdha DeshpandeDepartment of Biology, Brandeis University, Waltham, MA 02453.
Reazur RahmanDepartment of Biology, Brandeis University, Waltham, MA 02453.
Hannah SuibDepartment of Biology, Brandeis University, Waltham, MA 02453.
Avital A RodalDepartment of Biology, Brandeis University, Waltham, MA 02453.ORCID 0000-0002-2051-8304
Michael RosbashDepartment of Biology, Brandeis University, Waltham, MA 02453; rosbash@brandeis.edu paradis@brandeis.edu.
Suzanne ParadisDepartment of Biology, Brandeis University, Waltham, MA 02453; rosbash@brandeis.edu paradis@brandeis.edu.
Brandeis University · USHoward Hughes Medical Institute · US

Funding

Semaphorin-Dependent GABAergic Synapse Formation: A Novel Approach to Increasing Inhibition in the Intact BrainR01NS065856 · NINDS · BRANDEIS UNIVERSITY · PI PARADIS, SUZANNE · 2010 to 2024
$5.4M
Roles of Recycling Endosomes in Neuronal Extracellular Vesicle Cargo TrafficR01NS103967 · NINDS · BRANDEIS UNIVERSITY · PI Avital Adah Rodal · 2018 to 2026
$4.5M
A new tool for the cell-specific identification of RNA binding protein targetsR01DA037721 · NIDA · BRANDEIS UNIVERSITY · PI ROSBASH, MICHAEL · 2013 to 2021
$2.4M
Transposon landscapes and transcriptome diversity in aging neuronsR01AG052465 · NIA · BRANDEIS UNIVERSITY · PI LAU, NELSON C · 2016 to 2020
$2.0M
Semaphorin-dependent GABAergic synapse formation: A novel approach to increasing inhibition in the intact brainR56NS065856 · NINDS · BRANDEIS UNIVERSITY · PI PARADIS, SUZANNE · 2020 to 2020
$614k
NIA NIH HHS R01 AG052465NIDA NIH HHS R01 DA037721NINDS NIH HHS R01 NS065856NINDS NIH HHS R01 NS103967NINDS NIH HHS R56 NS065856
6 · The paper itself

Abstract

Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are two related neurodegenerative diseases that present with similar TDP-43 pathology in patient tissue. TDP-43 is an RNA-binding protein which forms aggregates in neurons of ALS and FTD patients as well as in a subset of patients diagnosed with other neurodegenerative diseases. Despite our understanding that TDP-43 is essential for many aspects of RNA metabolism, it remains obscure how TDP-43 dysfunction contributes to neurodegeneration. Interestingly, altered neuronal dendritic morphology is a common theme among several neurological disorders and is thought to precede neurodegeneration. We previously found that both TDP-43 overexpression (OE) and knockdown (KD) result in reduced dendritic branching of cortical neurons. In this study, we used TRIBE (targets of RNA-binding proteins identified by editing) as an approach to identify signaling pathways that regulate dendritic branching downstream of TDP-43. We found that TDP-43 RNA targets are enriched for pathways that signal to the CREB transcription factor. We further found that TDP-43 dysfunction inhibits CREB activation and CREB transcriptional output, and restoring CREB signaling rescues defects in dendritic branching. Finally, we demonstrate, using RNA sequencing, that TDP-43 OE and KD cause similar changes in the abundance of specific messenger RNAs, consistent with their ability to produce similar morphological defects. Our data therefore provide a mechanism by which TDP-43 dysfunction interferes with dendritic branching, and may define pathways for therapeutic intervention in neurodegenerative diseases.

Indexed as

Cyclic AMP Response Element-Binding ProteinDendritesDNA-Binding ProteinsSignal TransductionAnimalsGene Expression RegulationHEK293 CellsHumansRatsRNA, MessengerTDP-43 ProteinopathiesCREB1 protein, humanCyclic AMP Response Element-Binding ProteinDNA-Binding ProteinsRNA, MessengerTARDBP protein, humanCREBTDP-43TRIBE

Identifiers

PMID32393629
PMCPMC7260973
OpenAlexW3022432356

What Socratic holds

Textmetadata
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 Socratic graph.