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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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
Imaging Intracellular Fluorescent Proteins at Nanometer Resolution
Betzig, E., Patterson, G. H., Sougrat, R., Lindwasser, O. W., Olenych, S. G., Bonifacino, J. S., Davidson, M. W., Lippincott‐Schwartz, J., & Hess, H. F. (2006) · Science · doi:10.1126/science.1127344 · Cited by 8,941
Lifeact: a versatile marker to visualize F-actin
Riedl, J., Crevenna, A. H., Kessenbrock, K., Yu, J. H., Neukirchen, D., Bista, M., Bradke, F., Jenne, D., Holak, T. A., Werb, Z., et al. (2008) · Nature Methods · doi:10.1038/nmeth.1220 · Cited by 2,189
Cells lying on a bed of microneedles: An approach to isolate mechanical force
Tan, J. L., Tien, J., Pirone, D. M., Gray, D. S., Bhadriraju, K., & Chen, C. S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0235407100 · Cited by 2,002
Actin Dynamics, Architecture, and Mechanics in Cell Motility
Blanchoin, L., Boujemaa‐Paterski, R., Sykes, C., & Plastino, J. (2014) · Physiological Reviews · doi:10.1152/physrev.00018.2013 · Cited by 1,547
Stretching Single Talin Rod Molecules Activates Vinculin Binding
Hernández, A. E. D. R., Pérez‐Jiménez, R., Liu, R., Roca‐Cusachs, P., Fernández, J. M., & Sheetz, M. P. (2009) · Science · doi:10.1126/science.1162912 · Cited by 1,492
Actin and Actin-Binding ProteinsPreprint
Pollard, T. D. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018226 · Cited by 1,023
Cell motility driven by actin polymerization
Mogilner, A., & OSTER, G. F. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79496-1 · Cited by 939
Actin cortex mechanics and cellular morphogenesis
Salbreux, G., Charras, G., & Paluch, E. K. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.07.001 · Cited by 898
Cellular motions and thermal fluctuations: the Brownian ratchet
Peskin, C. S., Odell, G. M., & OSTER, G. F. (1993) · Biophysical Journal · doi:10.1016/s0006-3495(93)81035-x · Cited by 896
Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex
Machesky, L. M., Mullins, R. D., Higgs, H. N., Kaiser, D. A., Blanchoin, L., May, R. C., Hall, M. E., & Pollard, T. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3739 · Cited by 773
Research works printed but not linked: 3
- Finer JT, 1995, Biophys. J., 68, 291
- Grimm HP, 2003, Meister J-J, 32, 563
- Wang Y, 2016, JoVE, 118, e54774
Cited by
Sorted by citations
Items 101–140 of 140
Broßell, D., Meyer-Plath, A., Gräb, O., Heunisch, E., Kämpf, K., Haase, A., & Wiemann, M. (2026) · Particle and Fibre Toxicology · doi:10.1186/s12989-026-00666-9 · Cited by 2
“3c) [32–34].”
FAST – filamentous actin segmentation tool for quantifying cytoskeletal organization
Aljapur, V., Gardner, A., Carayanniotis, J., & Harris, A. R. (2026) · Journal of Cell Science · doi:10.1242/jcs.264265 · Cited by 5
“…and lamellar networks, filopodia, stress fibers and focal adhesions, which are defined by the morphology of the structure, the organization of actin filaments within the structure, and the presence of specific actin regulatory proteins (Desroches and Harris, 2024; Harris et al., 2018).”
Self-citationStructural Biophysics of Cytoskeletal Force Transduction
Alushin, G. M., Connolly, S. M., & Njoku, B. C. (2026) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101223-022717 · Cited by 2
Bergeron-Sandoval, L.-P., Cai, A., Clouvel, A., Hitti, C., & Ehrlicher, A. J. (2022) · Frontiers in Physics · doi:10.3389/fphy.2022.890865 · Cited by 2
Nguyen, M. T., Ly, Q. K., Kim, H., & Lee, W. (2023) · Cells · doi:10.3390/cells13010009 · Cited by 2
Zhang, Y., Zhang, M., Zheng, J., Li, Z., Guo, Q., Chen, Y., Chen, Y., Jiang, X., & Tang, J. (2025) · ACS Nano · doi:10.1021/acsnano.5c09366 · Cited by 2
An Introduction to Material-based Mechanobiology
Nakanishi, J., & Uto, K. (2022) · Royal Society of Chemistry eBooks · doi:10.1039/9781839165375-00001 · Cited by 2
Ntetsika, M. (2021) · Computer Modeling in Engineering & Sciences · doi:10.32604/cmes.2021.017404 · Cited by 2
Scaffold stiffness affects oligodendrocyte proliferation via cell traction forces
Watanabe, H., Uyeda, A., Quan, L., Iwai, S., Zhang, Z., Umezu, S., Suzuki, T., & Muramatsu, R. (2025) · Biomaterials Science · doi:10.1039/d5bm00689a · Cited by 1
Strained actin binding by the Prickle2 LIM domains and their regulation in the full-length protein
Bejar-Padilla, V., Li, M., Stachowiak, J. C., & Wallingford, J. B. (2025) · Molecular Biology of the Cell · doi:10.1091/mbc.e25-05-0244 · Cited by 1
Yu, W., Liu, X., Liu, Y., Chen, X., Ge, S., & Dong, Z. (2025) · Advanced Functional Materials · doi:10.1002/adfm.202523349 · Cited by 1
The actin crosslinker Fimbrin is required for force sensing at tricellular junctions
Taneja, N., Looney, C. A., Moubarak, M. F., McGovern, M. J., Yeoh, K., & Zallen, J. A. (2026) · Developmental Cell · doi:10.1016/j.devcel.2026.07.001 · Cited by 4
Resource Letter BP-1: Biological physics
Parthasarathy, R. (2021) · American Journal of Physics · doi:10.1119/5.0060279 · Cited by 1
Inference of the force pattern acting on a semiflexible filament from shape analysis
Wenger, J., Brigante, A. M., Casafuz, A. B. F., Bruno, L., & Monastra, A. (2023) · Physical review. E · doi:10.1103/physreve.108.064402 · Cited by 1
Ly, Q. K., Nguyen, M. T., Ngo, T. H. P., & Lee, W. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252413564 · Cited by 1
Actin conformation dynamics precede force generation in cytotoxic T lymphocytes
Rochussen, A. M., Kebabci, A. O., Winkel, A. K., Franze, K., Fletcher, D. A., Griffiths, G. M., & Lippert, A. H. (2026) · Communications Biology · doi:10.1038/s42003-026-11011-3 · Cited by 1
“Visua-lising different F-actin conformations in living cells is possible via genetically encoded actin-binding proteins fused with fl uorescent proteins, with different probes binding to the cytoskeleton in varied ways 30 .”
Self-citationIntroducing the Mechanical Forces in Biochemistry Special Issue
Udgaonkar, J. B. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00999 · Cited by 1
Mechanics and Motility of Epithelial Cells: From Single Cell Behavior to Collective Migration
Skamrahl, M. (2023) · doi:10.53846/goediss-9668 · Cited by 1
ABM of osteoblast's mechanotransduction pathway: time patterns of critical eventsPreprint
Ascolani, G., Skerry, T. M., Lacroix, D. J., Dall’Ara, E., & Shuaib, A. (2019) · arXiv (Cornell University) · doi:10.48550/arxiv.1902.08707
“Indeed, the process becomes immediately much more complex when there are not only active and inactive states, but also interactions with other molecular species [4,5].”
BackgroundJiang, X. Z. (2018) · UCL Discovery (University College London)
Qu, C., Roth, R. A., Loitman, C., Hammad, D., Genin, G. M., Miner, J. H., & Suleiman, H. Y. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.29.428712
Jo, M. H., Li, J., Jaumouillé, V., Hao, Y., Coppola, J. D., Yan, J., Waterman, C. M., Springer, T. A., & Ha, T. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.08.495291
Stressed Actin Binding by the Prickle2 LIM Domains and its Regulation in the Full-Length ProteinPreprint
Bejar-Padilla, V., Li, M., Stachowiak, J. C., & Wallingford, J. B. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.30.657073
AI Uncovers the Rapid Activation of Catch-Bonds under Force
Melo, M. C. R., & Bernardi, R. C. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5c01181
Regulation of actin cytoskeleton by Ca2+-binding S100 proteins
Jurewicz, E., Moraczewska, J., & Filipek, A. (2025) · Cell Calcium · doi:10.1016/j.ceca.2025.103087 · Cited by 1
Wang, J., Yang, H., Ma, X., Liu, J., Li, L., Chen, L., & Wei, F. (2023) · Figshare · doi:10.6084/m9.figshare.22616401
Ascolani, G., Skerry, T. M., Lacroix, D. J., Dall’Ara, E., & Shuaib, A. (2020) · Figshare · doi:10.6084/m9.figshare.11998734
Wang, J., Yang, H., Ma, X., Liu, J., Li, L., Chen, L., & Wei, F. (2023) · Figshare · doi:10.6084/m9.figshare.22616404
Wang, J., Yang, H., Ma, X., Liu, J., Li, L., Chen, L., & Wei, F. (2023) · Figshare · doi:10.6084/m9.figshare.22616407
Contribution of actin cytoskeleton to C. elegans embryonic elongation
Lardennois, A. (2019) · theses.fr (ABES) · doi:10.70675/310f3c9az6375z44d3zabe6z662c048eb411
Role of intermediate filaments in mechanotransduction
Provenzano, G. D. (2021) · theses.fr (ABES) · doi:10.70675/dcc9ac33zf0b2z45b9zbd23z37f03e91208c
Actin Quantification Using the Filamentous Actin Segmentation Tool (FAST)
Aljapur, V., Gardner, A., Carayanniotis, J., & Harris, A. R. (2026) · BIO-PROTOCOL · doi:10.21769/bioprotoc.5765
Self-citationPlant actin networks are rapid mechano-adaptive scaffoldsPreprint
Lamers, J., Daamen, A., Pinto, A., Tauber, J., Gosselink, S., Borassi, C., Sen, U., van der Gucht, J., & Sprakel, J. H. B. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.16.738884
“In animals, actin also plays a central role in cellular mechanobiology ( 7 ).”
Han, Z., Wang, S.-H., & Huo, B. (2026) · Computer Methods in Biomechanics & Biomedical Engineering · doi:10.1080/10255842.2026.2724358
Zhu, Y., Liu, C., Backman, L. J., Zhang, W., & Chen, J. (2026) · Engineered Regeneration · doi:10.1016/j.engreg.2026.08.001
Lightsey, N. K., Fluskey, G., Cruz-Gonzalez, B., Fan, F., Saha, S., Hall, E., & Hanjaya‐Putra, D. (2026) · Cell Reports Methods · doi:10.1016/j.crmeth.2026.101574
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
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review