Non-sarcomeric mode of myosin II organization in the fibroblast lamellum.
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The organization of myosin in the fibroblast lamellum was studied by correlative fluorescence and electron microscopy after a novel procedure to reveal its underlying morphology. An X-rhodamine analog of conventional smooth muscle myosin (myosin II) that colocalized after microinjection with endogenous myosin was used to trace myosin distribution in living fibroblasts. Then, the same cells were examined by EM of platinum replicas. To visualize the structural arrangement of myosin, other cytoskeletal fibrillar structures had to be removed: microtubules were depolymerized by nocodazole treatment of the living cells before injection of myosin; continued nocodazole treatment also induced the intermediate filaments to concentrate near the nucleus, thus removing them from the lamellar region; actin filaments were removed after lysis of the cells by incubation of the cytoskeletons with recombinant gelsolin. Possible changes in myosin organization caused by this treatment were examined by fluorescence microscopy. No significant differences in myosin distribution patterns between nocodazole-treated and control cells were observed. Cell lysis and depletion of actin also did not induce reorganization of myosin as was shown by direct comparison of myosin distribution in the same cells in the living state and after gelsolin treatment. EM of the well-spread, peripheral regions of actin-depleted cytoskeletons revealed a network of bipolar myosin mini-filaments, contracting each other at their terminal, globular regions. The morphology of this network corresponded well to the myosin distribution observed by fluorescence microscopy. A novel mechanism of cell contraction by folding of the myosin filament network is proposed.
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Bounds of the bending force applied to the first anchor point were determined using literature values, resulting in P1 = Pmax = 0.12-2.25 nN.
“Bounds of the bending force applied to the first anchor point were determined using literature values for the force exerted by each active myosin-II dimer, the number of myosin-II dimers Nmyo per actin filament and the number of actin filaments in each stress filament Nactin (Eq. 3 in Appendix A) [35, 36], resulting in P1 = Pmax = 0.12–2.25 nN.”
From Macrophages bend long fibres with flexural rigidity lower than 3 mN·nm2 to avoid frustrated phagocytosis (2026) · cites this paper as [36]
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- Authors
- Verkhovsky, A. B., & Borisy, G. G.
- Affiliations
- Lomonosov Moscow State University (RU)
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1993-11-01
- Volume
- 123
- Issue
- 3
- Pages
- 637-652
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2200132
- OpenAlex
- W2108386137
- Cited by
- 141
- References
- 77
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 2 · 2023: 4 · 2022: 5 · 2021: 4 · 2020: 3 · 2019: 3 · 2018: 8 · 2017: 6 · 2016: 4 · 2015: 3 · 2014: 6 · 2013: 7 · 2012: 10
- FWCI
- 1.92
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- Lomonosov Moscow State University
- National Institutes of Health (RR00570, GM‐25062)
- National Institute of General Medical Sciences (GM 25062)
- National Center for Research Resources (RR-00570)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- myosin II, nocodazole, gelsolin, intermediate filaments, microtubules
- MeSH terms
- Actins, Animals, Cytoskeleton, Electrophoresis, Polyacrylamide Gel, Fibroblasts, Gizzard, Avian, Actin Cytoskeleton, Microinjections, Microscopy, Electron, Myosins, Rhodamines, Sarcomeres, Turkeys, 3T3 Cells, Mice
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