ArticleInterface focus2011
Non-muscle myosin II induces disassembly of actin stress fibres independently of myosin light chain dephosphorylation.
Article in Interface focus, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 47 citations in OpenAlex.
- Regionalized regulation of actomyosin organization influences cardiomyocyte cell shape changes during chamber curvature formation.Nature communications · 2026Article
- Endothelial Surface Glycocalyx in Vascular Functions and Diseases.Advances in experimental medicine and biology · 2026Review
- Enhancing suspended cell transfection by inducing localized distribution of the membrane actin cortex before exposure to electromechanical stimulation.Biotechnology letters · 2023Article
- A statistical mechanics model for determining the length distribution of actin filaments under cellular tensional homeostasis.Scientific reports · 2022Article
- Analysis of chemomechanical behavior of stress fibers by continuum mechanics-based FRAP.Biophysical journal · 2022Article
- Analysis of senescence-responsive stress fiber proteome reveals reorganization of stress fibers mediated by elongation factor eEF2 in HFF-1 cells.Molecular biology of the cell · 2022Article
- Article
- Deformable 96-well cell culture plate compatible with high-throughput screening platforms.PloS one · 2018Article
- A theory that predicts behaviors of disordered cytoskeletal networks.Molecular systems biology · 2017Article
- IFT88 influences chondrocyte actin organization and biomechanics.Osteoarthritis and cartilage · 2016Article
- Myosin II Activity Softens Cells in Suspension.Biophysical journal · 2015Article
- A biomechanical model for fluidization of cells under dynamic strain.Biophysical journal · 2015Article
- Endothelial surface glycocalyx can regulate flow-induced nitric oxide production in microvessels in vivo.PloS one · 2015Article
- Mechano-sensing and transduction by endothelial surface glycocalyx: composition, structure, and function.Wiley interdisciplinary reviews. Systems biology and medicineArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dynamic remodelling of actin stress fibres (SFs) allows non-muscle cells to adapt to applied forces such as uniaxial cell shortening. However, the mechanism underlying rapid and selective disassembly of SFs oriented in the direction of shortening remains to be elucidated. Here, we investigated how myosin crossbridge cycling induced by MgATP is associated with SF disassembly. Moderate concentrations of MgATP, or [MgATP], induced SF contraction. Meanwhile, at [MgATP] slightly higher than the physiological level, periodic actin patterns emerged along the length of SFs and dispersed within seconds. The actin fragments were diverse in length, but comparable to those in characteristic sarcomeric units of SFs. These results suggest that MgATP-bound non-muscle myosin II dissociates from the individual actin filaments that constitute the sarcomeric units, resulting in unbundling-induced disassembly rather than end-to-end actin depolymerization. This rapid SF disassembly occurred independent of dephosphorylation of myosin light chain. In terms of effects on actin-myosin interactions, a rise in [MgATP] is functionally equivalent to a temporal decrease in the total number of actin-myosin crossbridges. Actin-myosin crossbridges are known to be reduced by an assisting load on myosin. Thus, the present study suggests that reducing the number of actin-myosin crossbridges promotes rapid and orientation-dependent disassembly of SFs after cell shortening.
Indexed as
Identifiers
What OpenQuestion holds
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.