ArticleThe Journal of cell biology1993
Non-sarcomeric mode of myosin II organization in the fibroblast lamellum.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 144 citations in OpenAlex.
- Topological control of spontaneous failure in active nematic solids.Nature materials · 2026Article
- Macrophages bend long fibres with flexural rigidity lower than 3 mN·nmParticle and fibre toxicology · 2026Article
- β-adrenergic signaling modulates breast cancer cell mechanical behaviors through a RhoA-ROCK-myosin II axis.iScience · 2025Article
- Direct detection of deformation modes on varying length scales in active biopolymer networks.bioRxiv : the preprint server for biology · 2025Article
- Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024Review
- Nonmuscle myosin 2 filaments are processive in cells.Biophysical journal · 2023Article
- Non-muscle myosin 2 at a glance.Journal of cell science · 2023Review
- Non-muscle myosin 2 filaments are processive in cells.bioRxiv : the preprint server for biology · 2023Article
- F-actin architecture determines constraints on myosin thick filament motion.Nature communications · 2022Article
- Simulated actin reorganization mediated by motor proteins.PLoS computational biology · 2022Article
- Imaging Cytoskeleton Components by Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Ventral stress fibers induce plasma membrane deformation in human fibroblasts.Molecular biology of the cell · 2021Article
- Article
- Actin bundle architecture and mechanics regulate myosin II force generation.Biophysical journal · 2021Article
- Remarkable structural transformations of actin bundles are driven by their initial polarity, motor activity, crosslinking, and filament treadmilling.PLoS computational biology · 2019Article
- Molecular form and function of the cytokinetic ring.Journal of cell science · 2019Review
- Network Contractility During Cytokinesis-from Molecular to Global Views.Biomolecules · 2019Review
- Assembly of myosin II filament arrays: Network Contraction versus Expansion.Cytoskeleton (Hoboken, N.J.) · 2018Review
- Entropy production rate is maximized in non-contractile actomyosin.Nature communications · 2018Article
- Tunable structure and dynamics of active liquid crystals.Science advances · 2018Article
10 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.