Linking substrate and nucleus via actin cytoskeleton in pluripotency maintenance of mouse embryonic stem cells.


Journal

Stem cell research
ISSN: 1876-7753
Titre abrégé: Stem Cell Res
Pays: England
ID NLM: 101316957

Informations de publication

Date de publication:
12 2019
Historique:
received: 12 03 2019
revised: 13 09 2019
accepted: 08 10 2019
pubmed: 13 11 2019
medline: 3 6 2020
entrez: 13 11 2019
Statut: ppublish

Résumé

Pluripotency of mouse embryonic stem cells is regulated by transcription factor regulatory networks as well as mechanical stimuli sensed by the cells. It has been unclear how the mechanical strain applied to the plasma membrane is transferred to the nucleus in mouse embryonic stem cells (mESCs). We here investigated the machinery of the mechanotransduction based on the finding that spontaneous differentiation of mESCs was inhibited with the downregulation of ROCK2 in cells attached to soft substrates. On examining the effects of actin bindings to both focal adhesions and cell junctions in cells on soft substrates, co-localization of actin filaments and α-catenin, which links actin to E-cadherin, decreased after differentiation induction. Also, disrupting actin-nucleus mechanical link through dominant negative assay of Nesprins helps to sustain the pluripotency genes; thus, revealing that mechanical strain relayed by actin-Nesprin connection is required for the initiation of the differentiation process.

Identifiants

pubmed: 31715427
pii: S1873-5061(19)30244-2
doi: 10.1016/j.scr.2019.101614
pii:
doi:

Substances chimiques

Cadherins 0
alpha Catenin 0
Rock2 protein, mouse EC 2.7.11.1
rho-Associated Kinases EC 2.7.11.1

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

101614

Informations de copyright

Copyright © 2019 The Author(s). Published by Elsevier B.V. All rights reserved.

Auteurs

Brit Gracy David (BG)

RIKEN Center for Biosystems Dynamics Research (BDR), 6-2-3 Furuedai, Suita-shi, Osaka 565-0874, Japan; Graduate School of Frontier Bioscience, Osaka University, 1-3 Yamadaoka Suita-shi, Osaka, 565-0871, Japan.

Hideaki Fujita (H)

RIKEN Center for Biosystems Dynamics Research (BDR), 6-2-3 Furuedai, Suita-shi, Osaka 565-0874, Japan; Waseda Bioscience Research Institute in Singapore (WABIOS), 11 Biopolis Way, #05-02, Helios, 138667, Singapore.

Kyota Yasuda (K)

Graduate School of Integrated Sciences for Life, Hiroshima University, 1-3-2 Kagamiyama, Higashi-Hiroshima-shi, Hiroshima, 739-8511, Japan.

Kazuko Okamoto (K)

RIKEN Center for Biosystems Dynamics Research (BDR), 6-2-3 Furuedai, Suita-shi, Osaka 565-0874, Japan.

Yulia Panina (Y)

RIKEN Center for Biosystems Dynamics Research (BDR), 6-2-3 Furuedai, Suita-shi, Osaka 565-0874, Japan; Graduate School of Frontier Bioscience, Osaka University, 1-3 Yamadaoka Suita-shi, Osaka, 565-0871, Japan.

Junya Ichinose (J)

RIKEN Center for Biosystems Dynamics Research (BDR), 6-2-3 Furuedai, Suita-shi, Osaka 565-0874, Japan.

Osamu Sato (O)

Department of Cellular and Molecular Biology, University of Texas Health Science Center at Tyler, Tyler, TX75708, USA.

Masanobu Horie (M)

Radioisotope Research Center, Division of Biochemical Engineering, Kyoto University, Yoshida, Konoe-cho, Sakyo-ku, Kyoto, 606-8501, Japan.

Taro Ichimura (T)

RIKEN Center for Biosystems Dynamics Research (BDR), 6-2-3 Furuedai, Suita-shi, Osaka 565-0874, Japan; Department of Transdimensional Life Imaging, Open and Transdisciplinary Research Initiatives, Osaka University, 1-1 Yamadaoka, Suita, Osaka 565-0871, Japan.

Yasushi Okada (Y)

RIKEN Center for Biosystems Dynamics Research (BDR), 6-2-3 Furuedai, Suita-shi, Osaka 565-0874, Japan; Department of Physics, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.

Tomonobu M Watanabe (TM)

RIKEN Center for Biosystems Dynamics Research (BDR), 6-2-3 Furuedai, Suita-shi, Osaka 565-0874, Japan. Electronic address: tomowatanabe@riken.jp.

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Classifications MeSH