Evidence map›Paper›PMID 31912196›Full record

ArticleCellular and molecular life sciences : CMLS2020

Dynein-mediated nuclear translocation of yes-associated protein through microtubule acetylation controls fibroblast activation.

Eunae You, Panseon Ko, Jangho Jeong, Seula Keum, Jung-Woong Kim, Young-Jin Seo, Woo Keun Song, Sangmyung Rhee

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
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  4. Mechanochemistry: Fundamental Principles and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  14. The role of the cytoskeleton in fibrotic diseases.Frontiers in cell and developmental biology · 2024
    Review
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  16. Article
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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

8 authors at 3 institutions in 1 country.

Eunae YouDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Panseon KoDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Jangho JeongDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Seula KeumDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Jung-Woong KimDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Young-Jin SeoDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Woo Keun SongBio Imaging and Cell Logistics Research Center, School of Life Sciences, Gwangju Institute of Science and Technology, 123 Cheomdangwagi-ro, Buk-Gu, Gwangju, 61005, Republic of Korea. wksong@gist.ac.kr.
Sangmyung RheeDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea. sangmyung.rhee@cau.ac.kr.ORCID http://orcid.org/0000-0003-2733-2147
Chung-Ang University · KRGwangju Institute of Science and Technology · KRSangmyung University · KR

Funding

Ministry of Health and Welfare HI17C1620National Research Foundation of Korea NRF-2017R1A2B4004324
6 · The paper itself

Abstract

Myofibroblasts are the major cell type that is responsible for increase in the mechanical stiffness in fibrotic tissues. It has well documented that the TGF-β/Smad axis is required for myofibroblast differentiation under the rigid substrate condition. However, the mechanism driving myofibroblast differentiation in soft substrates remains unknown. In this research, we demonstrated that interaction of yes-associated protein (YAP) and acetylated microtubule via dynein, a microtubule motor protein drives nuclear localization of YAP in the soft matrix, which in turn increased TGF-β1-induced transcriptional activity of Smad for myofibroblast differentiation. Pharmacological and genetical disruption of dynein impaired the nuclear translocation of YAP and decreased the TGF-β1-induced Smad activity even though phosphorylation and nuclear localization of Smad occurred normally in α-tubulin acetyltransferase 1 (α-TAT1) knockout cell. Moreover, microtubule acetylation prominently appeared in the fibroblast-like cells nearby the blood vessel in the fibrotic liver induced by CCl

Indexed as

AcetylationAdaptor Proteins, Signal TransducingAnimalsCell Cycle ProteinsCell DifferentiationCell LineCell NucleusDyneinsFibroblastsHEK293 CellsHumansMaleMice, Inbred C57BLMicrotubulesPhosphorylationProtein TransportAdaptor Proteins, Signal TransducingCell Cycle ProteinsDyneinsSmad ProteinsTransforming Growth Factor beta1Yap1 protein, mouseYAP-Signaling ProteinsECM stiffnessLiver fibrosisMicrotubule acetylationMyofibroblastSmadTGF-β1YAP

Identifiers

PMID31912196
PMCPMC11105004
OpenAlexW2999751113

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.