The DOI matches its Crossref record; 101 of the 101 references it cites were found in a registry or an index.
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]
Citations
Cites
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Cited by
Sorted by citations
Yi, B., Xu, Q., & Liu, W. X. (2021) · Bioactive Materials · doi:10.1016/j.bioactmat.2021.12.005 · Cited by 319
The role of the cell nucleus in mechanotransduction
Janota, C. S., Calero-Cuenca, F. J., & Gomes, E. R. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.03.001 · Cited by 156
Endothelial mechanobiology in atherosclerosis
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“It has become apparent that this coordination emerges largely as a result of deep interactions between biochemical signaling, cytoskeletal dynamics, and forces, each having been shown to modulate the other two (Hannezo and Heisenberg, 2019; Harris et al., 2018).”
BackgroundArgentati, C., Morena, F., Tortorella, I., Bazzucchi, M., Porcellati, S., Emiliani, C., & Martino, S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215337 · Cited by 143
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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