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Mechanotransduction by the Actin Cytoskeleton: Converting Mechanical Stimuli into Biochemical Signals
Abstract
Force transmission through the actin cytoskeleton plays a central role in cell movements, shape change, and internal organization. Dynamic reorganization of actin filaments by an array of specialized binding proteins creates biochemically and architecturally distinct structures, many of which are finely tuned to exert or resist mechanical loads. The molecular complexity of the actin cytoskeleton continues to be revealed by detailed biochemical assays, and the architectural diversity and dynamics of actin structures are being uncovered by advances in super-resolution fluorescence microscopy and electron microscopy. However, our understanding of how mechanical forces feed back on cytoskeletal architecture and actin-binding protein organization is comparatively limited. In this review, we discuss recent work investigating how mechanical forces applied to cytoskeletal proteins are transduced into biochemical signals. We explore multiple mechanisms for mechanical signal transduction, including the mechanosensitive behavior of actin-binding proteins, the effect of mechanical force on actin filament dynamics, and the influence of mechanical forces on the structure of single actin filaments. The emerging picture is one in which the actin cytoskeleton is defined not only by the set of proteins that constitute a network but also by the constant interplay of mechanical forces and biochemistry.
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“Stress filaments consist of actin, myosin-II dimers, and associated crosslinkers (Fig. 3c) [32–34].”
From Macrophages bend long fibres with flexural rigidity lower than 3 mN·nm2 to avoid frustrated phagocytosis (2026) · cites this paper as [34]
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Kim, D. S., Cheah, J. S., Lai, T. W., Zhao, K. X., Foust, S. R., Lee, Y. J., Lo, S. H., Heinrich, V., & Yamada, S. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114480 · Cited by 9
Modeling stem cell nucleus mechanics using confocal microscopy
Kennedy, Z., Newberg, J., Goelzer, M. H., Judex, S., Fitzpatrick, C. K., & Uzer, G. (2021) · Biomechanics and Modeling in Mechanobiology · doi:10.1007/s10237-021-01513-w · Cited by 9
Actin-membrane linkers: Insights from synthetic reconstituted systems
Tsai, F., Guérin, G., Pernier, J., & Bassereau, P. M. (2024) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2024.151402 · Cited by 10
Registry Kinetics of Myosin Motor Stacks Driven by Mechanical Force-Induced Actin Turnover
Dasbiswas, K., Hu, S., Bershadsky, A. D., & Safran, S. A. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.07.040 · Cited by 9
“Actin, like many other biological macromolecules, is mechanosensitive, in that its structural conformations are modulated by the mechanical forces acting on it (19).”
BackgroundElasticity of dense actin networks produces nanonewton protrusive forcesPreprint
Jasnin, M., Hervy, J., Balor, S., Bouissou, A., Proag, A., Voituriez, R., Maridonneau‐Parini, I., Baumeister, W. P., Dmitrieff, S., & Poincloux, R. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.13.439622 · Cited by 9
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The Shot CH1 domain recognises a distinct form of F-actin during Drosophila oocyte determination
Nashchekin, D., Squires, I. J., Prokop, A., & Johnston, D. S. (2024) · Development · doi:10.1242/dev.202370 · Cited by 9
“Changes in the helical twist of F-actin filaments can be caused by mechanical tension, by interactions with actin-binding proteins (Harris et al., 2018; Jégou and Romet-Lemonne, 2020; Harris et al., 2020), or by the bending of F-actin filaments promoted by differences in the nucleotide states of actin monomers (Reynol…”
BackgroundThe Actomyosin Cortex of Cells: A Thin Film of Active Matter
Kumar, K. V. (2021) · Journal of the Indian Institute of Science · doi:10.1007/s41745-020-00220-2 · Cited by 8
“The molecular field conjugate to (8) σ o = ν (”
BackgroundBiophysical cues involved in the stem cell niche for stemness maintenance
Li, C., Zheng, L., & Fan, Y. (2024) · Medicine in Novel Technology and Devices · doi:10.1016/j.medntd.2024.100301 · Cited by 7
An open-source combined atomic force microscope and optical microscope for mechanobiology studies
Delgado, D., Desroches, S., Kang, G., Aldabii, Y., & Harris, A. R. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e38214 · Cited by 7
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“89,90 Furthermore, loss of the LINC complex causes nucleo-cytoplasmic mechanical uncoupling, impairing cellular responses to mechanical stimuli and leading to nuclear morphological abnormalities and gene misregulation.”
Thermosensory Spiking Activity of Proteinoid Microspheres Cross-Linked by Actin Filaments
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“118 − 121 Localization models the physical connectivity between inputs and outputs in the same way that neural signaling follows protected wire transmission pathways.”
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Capturing ovarian dynamics through spatial profiling of the mechano-microenvironment
Tomida, K., Ong, H. T., Young, J. L., & Chan, C. J. (2025) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2025.103642 · Cited by 6
Tissue-Informed Biomaterial Innovations Advance Pulmonary Regenerative Engineering
Kary, A. D., Noelle, H., & Magin, C. M. (2025) · ACS Macro Letters · doi:10.1021/acsmacrolett.5c00075 · Cited by 5
Ascolani, G., Skerry, T. M., Lacroix, D. J., Dall’Ara, E., & Shuaib, A. (2020) · BMC Bioinformatics · doi:10.1186/s12859-020-3394-0 · Cited by 5
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Develop Tandem Tension Sensor to Gauge Integrin-Transmitted Molecular Forces
Niraula, G., Pyne, A., & Wang, X. (2024) · ACS Sensors · doi:10.1021/acssensors.4c00756 · Cited by 4
Song, M., & Kwon, S. (2021) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-021-0070-9 · Cited by 3
“Mechano-transduction has a central role in cell migration, cell shape, and tissue morphogenesis by converting mechanical stimuli into biochemical responses acting through the actin cytoskeleton [33].”
BackgroundWang, J., Li, M., Wu, W., Zhang, H., Yang, Y., Usman, M., Aernouts, B., Loor, J. J., & Xu, C. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c04421 · Cited by 3
Metadata
- Authors
- Harris, A. R., Jreij, P., & Fletcher, D. A.
- Affiliations
- University of California, Berkeley (US)
- Lawrence Berkeley National Laboratory (US)
- Venue
- Annual Review of Biophysics
- Publisher
- Annual Reviews
- Published
- 2018-05-20
- Volume
- 47
- Issue
- 1
- Pages
- 617-631
- ISSN
- 1936-122X (ISSN-L)
- 1936-1238
- OpenAlex
- W2803134496
- Cited by
- 140
- References
- 101
- Citations by year
- 2026: 10 · 2025: 16 · 2024: 19 · 2023: 14 · 2022: 14 · 2021: 24 · 2020: 25 · 2019: 15 · 2018: 3
- FWCI
- 1.88
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Biophysics (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- mechanotransduction, actin cytoskeleton, mechanical forces, actin-binding proteins, actin filament dynamics, actin filament structure, force transmission, mechanical signal transduction, cytoskeletal structure, cell mechanics
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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