Evidence map›Paper›PMID 32046944›Full record

ArticleRedox biology2020

Distinct dual roles of p-Tyr42 RhoA GTPase in tau phosphorylation and ATP citrate lyase activation upon different Aβ concentrations.

Kim Cuong Cap, Yeon-Joo Jung, Bo Young Choi, Seung Jae Hyeon, Jae-Gyu Kim, Jung-Ki Min, Rokibul Islam, Abu Jubayer Hossain, Won-Suk Chung, Sang Won Suh and 2 more

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2020. 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
2.2field-weighted citation impact, top 12% 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, 28 citations in OpenAlex.

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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

12 authors at 6 institutions in 3 countries.

Kim Cuong CapDepartment of Biochemistry, Hallym University College of Medicine, Chuncheon, Kangwon-do, 24252, Republic of Korea; Institute of Research and Development, Duy Tan University, Danang, 550000, Viet Nam.
Yeon-Joo JungDepartment of Biological Science, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Republic of Korea.
Bo Young ChoiDepartment of Physiology, Hallym University College of Medicine, Chuncheon, Kangwon-do, 24252, Republic of Korea.
Seung Jae HyeonLaboratory for Brain Gene Regulation and Epigenetics, Center for Neuromedicine, Brain Science Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.
Jae-Gyu KimDepartment of Biochemistry, Hallym University College of Medicine, Chuncheon, Kangwon-do, 24252, Republic of Korea; Institute of Cell Differentiation and Aging, Hallym University College of Medicine, Chuncheon, Kangwon-do, 24252, Republic of Korea.
Jung-Ki MinDepartment of Biochemistry, Hallym University College of Medicine, Chuncheon, Kangwon-do, 24252, Republic of Korea.
Rokibul IslamDepartment of Biochemistry, Hallym University College of Medicine, Chuncheon, Kangwon-do, 24252, Republic of Korea; Department of Biotechnology and Genetic Engineering, Faculty of Biological Science, Islamic University, Kushtia, 7003, Bangladesh.
Abu Jubayer HossainDepartment of Biochemistry, Hallym University College of Medicine, Chuncheon, Kangwon-do, 24252, Republic of Korea.
Won-Suk ChungDepartment of Biological Science, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Republic of Korea.
Sang Won SuhDepartment of Physiology, Hallym University College of Medicine, Chuncheon, Kangwon-do, 24252, Republic of Korea.
Hoon RyuLaboratory for Brain Gene Regulation and Epigenetics, Center for Neuromedicine, Brain Science Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.
Jae-Bong ParkDepartment of Biochemistry, Hallym University College of Medicine, Chuncheon, Kangwon-do, 24252, Republic of Korea; Institute of Cell Differentiation and Aging, Hallym University College of Medicine, Chuncheon, Kangwon-do, 24252, Republic of Korea; Hallym Clinical and Translational Science Institute, Hallym University College of Medicine, Chuncheon, Kangwon-do, 24252, Republic of Korea; eLmed Co., Hallym University College of Medicine, Chuncheon, Kangwon-do, 24252, Republic of Korea. Electronic address: jbpark@hallym.ac.kr.
Hallym University · KRKorea Advanced Institute of Science and Technology · KRDuy Tan University · VNIslamic University · BDKorea Institute of Brain Science · KRKorea Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Both the accumulation of Amyloid-β (Aβ) in plaques and phosphorylation of Tau protein (p-Tau) in neurofibrillary tangles have been identified as two major symptomatic features of Alzheimer's disease (AD). Despite of critical role of Aβ and p-Tau in AD progress, the interconnection of signalling pathways that Aβ induces p-Tau remains elusive. Herein, we observed that a popular AD model mouse (APP/PS1) and Aβ-injected mouse showed an increase in p-Tyr42 Rho in hippocampus of brain. Low concentrations of Aβ (1 μM) induced RhoA-mediated Ser422 phosphorylation of Tau protein (p-Ser422 Tau), but reduced the expression of ATP citrate lyase (ACL) in the HT22 hippocampal neuronal cell line. In contrast, high concentrations of Aβ (10 μM) along with high levels of superoxide production remarkably attenuated accumulation of p-Ser422 Tau, but augmented ACL expression and activated sterol regulatory element-binding protein 1 (SREBP1), leading to cellular senescence. Notably, a high concentration of Aβ (10 μM) induced nuclear localization of p-Tyr42 Rho, which positively regulated NAD kinase (NADK) expression by binding to the NADK promoter. Furthermore, severe AD patient brain showed high p-Tyr42 Rho levels. Collectively, our findings indicate that both high and low concentrations of Aβ are detrimental to neurons via distinct two p-Tyr42 RhoA-mediated signalling pathways in Ser422 phosphorylation of Tau and ACL expression.

Indexed as

Alzheimer Diseasetau ProteinsAmyloid beta-PeptidesAnimalsATP Citrate (pro-S)-LyaseHumansMiceMice, TransgenicPhosphorylationrhoA GTP-Binding ProteinAmyloid beta-PeptidesATP Citrate (pro-S)-LyaserhoA GTP-Binding ProteinRHOA protein, humantau ProteinsACLAlzheimer diseaseAβNADKp-Taup-Tyr42 RhoASuperoxide

Identifiers

PMID32046944
PMCPMC7264465
OpenAlexW3003535156

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.