What factors determine the number of nonmuscle myosin II in the sarcomeric unit of stress fibers?


Journal

Biomechanics and modeling in mechanobiology
ISSN: 1617-7940
Titre abrégé: Biomech Model Mechanobiol
Pays: Germany
ID NLM: 101135325

Informations de publication

Date de publication:
Feb 2021
Historique:
received: 15 05 2020
accepted: 01 08 2020
pubmed: 11 8 2020
medline: 14 10 2021
entrez: 11 8 2020
Statut: ppublish

Résumé

Actin stress fibers (SFs), a contractile apparatus in nonmuscle cells, possess a contractile unit that is apparently similar to the sarcomere of myofibrils in muscles. The function of SFs has thus often been addressed based on well-characterized properties of muscles. However, unlike the fixed number of myosin molecules in myofibrils, the number of nonmuscle myosin II (NMII) within the contractile sarcomeric unit in SFs is quite low and variable for some reason. Here we address what factors may determine the specific number of NMII in SFs. We suggest with a theoretical model that the number lies just in between the function of SFs for bearing cellular tension under static conditions and for promptly disintegrating upon forced cell shortening. We monitored shortening-induced disintegration of SFs in human osteosarcoma U2OS cells expressing mutants of myosin regulatory light chain that virtually regulates the interaction of NMII with actin filaments, and the behaviors observed were indeed consistent with the theoretical consequences. This situation-specific nature of SFs may allow nonmuscle cells to respond adaptively to mechanical stress to circumvent activation of pro-inflammatory signals as previously indicated, i.e., a behavior distinct from that of muscles that are basically specialized for exhibiting contractile activity.

Identifiants

pubmed: 32776260
doi: 10.1007/s10237-020-01375-8
pii: 10.1007/s10237-020-01375-8
doi:

Substances chimiques

Myosin Light Chains 0
Myosin Type II EC 3.6.1.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

155-166

Subventions

Organisme : Japan Society for the Promotion of Science
ID : 18H03518
Organisme : Japan Society for the Promotion of Science
ID : 19K22967

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Auteurs

Takumi Saito (T)

Division of Bioengineering, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka, 560-8531, Japan.
Japan Society for the Promotion of Science, Tokyo, Japan.

Wenjing Huang (W)

Department of Bioengineering, Graduate School of Engineering, The University of Tokyo, Tokyo, Japan.

Tsubasa S Matsui (TS)

Division of Bioengineering, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka, 560-8531, Japan.

Masahiro Kuragano (M)

Graduate School of Engineering, Muroran Institute of Technology, Muroran, Japan.

Masayuki Takahashi (M)

Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo, Japan.

Shinji Deguchi (S)

Division of Bioengineering, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka, 560-8531, Japan. deguchi@me.es.osaka-u.ac.jp.

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