Evidence map›Paper›PMID 31690171›Full record

ArticleAutophagy2020

PTK2/FAK regulates UPS impairment via SQSTM1/p62 phosphorylation in TARDBP/TDP-43 proteinopathies.

Shinrye Lee, Yu-Mi Jeon, Sun Joo Cha, Seyeon Kim, Younghwi Kwon, Myungjin Jo, You-Na Jang, Seongsoo Lee, Jaekwang Kim, Sang Ryong Kim and 4 more

Open access · greenAbstract read
In one paragraph

Article in Autophagy, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 52 citations in OpenAlex.

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  16. Invertebrate genetic models of amyotrophic lateral sclerosis.Frontiers in molecular neuroscience · 2024
    Review
  17. Article
  18. Review
  19. Article
  20. Frontiers in neuroscience · 2023
    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

14 authors at 3 institutions in 1 country.

Shinrye LeeDementia Research Group, Korea Brain Research Institute (KBRI) , Daegu, South Korea.
Yu-Mi JeonDementia Research Group, Korea Brain Research Institute (KBRI) , Daegu, South Korea.
Sun Joo ChaSoonchunhyang Institute of Medi-bio Science, Soonchunhyang University , Cheonan, South Korea.
Seyeon KimDementia Research Group, Korea Brain Research Institute (KBRI) , Daegu, South Korea.
Younghwi KwonDementia Research Group, Korea Brain Research Institute (KBRI) , Daegu, South Korea.
Myungjin JoDementia Research Group, Korea Brain Research Institute (KBRI) , Daegu, South Korea.
You-Na JangNeural circuits Research Group, Korea Brain Research Institute (KBRI) , Daegu, South Korea.
Seongsoo LeeGwangju Center, Korea Basic Science Institute (KBSI) , Gwangju, South Korea.
Jaekwang KimDementia Research Group, Korea Brain Research Institute (KBRI) , Daegu, South Korea.
Sang Ryong KimSchool of Life Sciences, BK21 Plus KNU Creative BioResearch Group, Institute of Life Science & Biotechnology, Kyungpook National University , Daegu, South Korea.ORCID 0000-0003-0299-1613
Kea Joo LeeNeural circuits Research Group, Korea Brain Research Institute (KBRI) , Daegu, South Korea.ORCID 0000-0002-1366-4709
Sung Bae LeeDepartment of Brain & Cognitive Sciences, DGIST , Daegu, South Korea.ORCID 0000-0002-8980-6769
Kiyoung KimSoonchunhyang Institute of Medi-bio Science, Soonchunhyang University , Cheonan, South Korea.
Hyung-Jun KimDementia Research Group, Korea Brain Research Institute (KBRI) , Daegu, South Korea.
Daegu Gyeongbuk Institute of Science and Technology · KRKorea Brain Research Institute · KRSoonchunhyang University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TARDBP/TDP-43 (TAR DNA binding protein) proteinopathies are a common feature in a variety of neurodegenerative disorders, including amyotrophic lateral sclerosis (ALS), frontotemporal lobar degeneration (FTLD), and Alzheimer disease (AD). However, the molecular mechanisms underlying TARDBP-induced neurotoxicity are largely unknown. In this study, we demonstrated that TARDBP proteinopathies induce impairment in the ubiquitin proteasome system (UPS), as evidenced by an accumulation of ubiquitinated proteins and a reduction in proteasome activity in neuronal cells. Through kinase inhibitor screening, we identified PTK2/FAK (PTK2 protein tyrosine kinase 2) as a suppressor of neurotoxicity induced by UPS impairment. Importantly, PTK2 inhibition significantly reduced ubiquitin aggregates and attenuated TARDBP-induced cytotoxicity in a

Indexed as

Unfolded Protein ResponseAnimalsAutophagyBehavior, AnimalDNA-Binding ProteinsDown-RegulationDrosophila melanogasterFocal Adhesion Kinase 1MiceModels, BiologicalMutationNeurotoxinsPhosphorylationPhosphoserineProtein Serine-Threonine KinasesSequestosome-1 ProteinDNA-Binding ProteinsFocal Adhesion Kinase 1NeurotoxinsPhosphoserineProtein Serine-Threonine KinasesSequestosome-1 ProteinTardbp protein, mouseTbk1 protein, mouseUbiquitinated ProteinsAmyotrophic lateral sclerosisPTK2/FAKSQSTM1/p62TARDBP/TDP-43ubiquitin-proteasome system

Identifiers

PMID31690171
PMCPMC7469499
OpenAlexW2985969718

What OpenQuestion 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 OpenQuestion graph.