Detail of Fig7E_ACTKDonGel_0207_7



Project
Title
Phase contrast images of alpha-actinin knockdown C2C12 cell migration on gel
Description
Z-series and time-lapse images of actinin knockdown C2C12 cell dynamics for up to 240 minutes. C2C12 cell were cultured on polyacrylamide gel substrates.
Release, Updated
2025-04-10
License
CC BY
Kind
Image data
File Formats
.ics, .ids
Data size
160.2 MB

Organism
Mus musculus ( NCBI:txid10090 )
Strain(s)
-
Cell Line
C2C12 cell

Datatype
-
Molecular Function (MF)
Biological Process (BP)
cell migration
Cellular Component (CC)
Biological Imaging Method
confocal microscopy ( Fbbi:00000251 )
time lapse microscopy ( Fbbi:00000249 )
X scale
0.44 micrometer/pixel
Y scale
0.44 micrometer/pixel
Z scale
2 micrometer
T scale
10 minutes

Image Acquisition
Experiment type
-
Microscope type
-
Acquisition mode
-
Contrast method
-
Microscope model
-
Detector model
-
Objective model
-
Filter set
-

Summary of Methods
Katsuta H, Okuda S, Nagayama K, Machiyama H, Kidoaki S, Kato M, Sokabe M, Miyata T, Hirata H. Actin crosslinking by alpha-actinin averts viscous dissipation of myosin force transmission in stress fibers. iScience. 2023 Feb1;26(3):106090.
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
Hiroaki Hirata , Kanazawwa Institute of Technology
Contributors
Hiroki Katsuta, Satoru Okuda, Kazuaki Nagayama, Hiroaki Machiyama, Hiroaki Hirata

OMERO Dataset
-
OMERO Project
Source