Summary of ssbd-repos-000292

SSBD:database
URL

Name
ssbd-repos-000292 (292-Katsuta-StressFiber)
URL
DOI
-

Title
Time-lapse images showing the pivotal role of alpha-actinin which generates mechanical force in stress fibers
Description
-
Submited Date
-
Release Date
2025-04-10
Updated Date
-
License
Funding information
-
File formats
Data size
20.9 GB

Organism
Mus musculus
Strain
-
Cell Line
C2C12 cell
Genes
-
Proteins
-

GO Molecular Function (MF)
actin filament binding
GO Biological Process (BP)
actin nucleation, regulation of stress fiber assembly, cell migration
GO Cellular Component (CC)
stress fiber, cell surface, cytoskeleton
Study Type
-
Imaging Methods
atomic force microscopy, confocal microscopy, time lapse microscopy, FRAP

Method Summary
-
Related paper(s)

Hiroki Katsuta, Satoru Okuda, Kazuaki Nagayama, Hiroaki Machiyama, Satoru Kidoaki, Masashi Kato, Masahiro Sokabe, Takaki Miyata, Hiroaki Hirata (2023) Actin crosslinking by alpha-actinin averts viscous dissipation of myosin force transmission in stress fibers., iScience, Volume 26, Number 3, pp. 106090

Published in 2023 Mar 17 (Electronic publication in Feb. 1, 2023, midnight )

(Abstract) Contractile force generated in actomyosin stress fibers (SFs) is transmitted along SFs to the extracellular matrix (ECM), which contributes to cell migration and sensing of ECM rigidity. In this study, we show that efficient force transmission along SFs relies on actin crosslinking by alpha-actinin. Upon reduction of alpha-actinin-mediated crosslinks, the myosin II activity induced flows of actin filaments and myosin II along SFs, leading to a decrease in traction force exertion to ECM. The fluidized SFs maintained their cable integrity probably through enhanced actin polymerization throughout SFs. A computational modeling analysis suggested that lowering the density of actin crosslinks caused viscous slippage of actin filaments in SFs and, thereby, dissipated myosin-generated force transmitting along SFs. As a cellular scale outcome, alpha-actinin depletion attenuated the ECM-rigidity-dependent difference in cell migration speed, which suggested that alpha-actinin-modulated SF mechanics is involved in the cellular response to ECM rigidity.

Contact(s)
Hiroaki Hirata
Organization(s)
Kanazawwa Institute of Technology
Image Data Contributors
Quantitative Data Contributors

Download files
Download zipped files