Epithelial morphogenesis depends on coordinated changes in cell shape, a process that is still poorly understood. During zebrafish epiboly and Drosophila dorsal closure, cell-shape changes at the epithelial margin are of critical importance. Here evidence is provided for a conserved mechanism of local actin and myosin 2 recruitment during theses events. It was found that during epiboly of the zebrafish embryo, the movement of the outer epithelium (enveloping layer) over the yolk cell surface involves the constriction of marginal cells. This process depends on the recruitment of actin and myosin 2 within the yolk cytoplasm along the margin of the enveloping layer. Actin and myosin 2 recruitment within the yolk cytoplasm requires the Ste20-like kinase Msn1, an orthologue of Drosophila Misshapen. Similarly, in Drosophila, actin and myosin 2 localization and cell constriction at the margin of the epidermis mediate dorsal closure and are controlled by Misshapen. Thus, this study has characterized a conserved mechanism underlying coordinated cell-shape changes during epithelial morphogenesis.
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http://dx.doi.org/10.1242/dev.02439 | DOI Listing |
PLoS Biol
January 2025
Department of Biomedical and Translational Sciences, Macon & Joan Brock Virginia Health Sciences at Old Dominion University, Norfolk, Virginia, United States of America.
Every heartbeat depends on cyclical contraction-relaxation produced by the interactions between myosin-containing thick and actin-based thin filaments (TFs) arranged into a crystalline-like lattice in the cardiac sarcomere. Therefore, the maintenance of thin filament length is crucial for myocardium function. The thin filament is comprised of an actin backbone, the regulatory troponin complex and tropomyosin that controls interactions between thick and thin filaments.
View Article and Find Full Text PDFJ Cell Sci
January 2025
Institute of Integrative Cell Biology and Physiology, University of Münster, 48149 Münster, Germany.
The actin-based motor myosin-19 (Myo19) exerts force on mitochondrial membrane receptors Miro1/2, influencing endoplasmic reticulum (ER)-mitochondria contact sites and mitochondrial cristae structure. The Mitochondrial Intermembrane Bridging (MIB) complex connects the outer and inner mitochondrial membranes at the cristae junction through the MICOS system. However, the interaction between Myo19, Miro1/2, and the MIB/MICOS complex in cristae regulation remains unclear.
View Article and Find Full Text PDFUnlabelled: Experimental studies have demonstrated that nutritional changes during development can result in phenotypic changes to mammalian cheek teeth. This developmental plasticity of tooth morphology is an example of phenotypic plasticity. Because tooth development occurs through complex interactions between manifold processes, there are many potential mechanisms which can contribute to a tooth's norm of reaction.
View Article and Find Full Text PDFFood Chem
January 2025
College of Food and Bioengineering, Xihua University, Chengdu 610039, China; Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, Chengdu 610039, China; School of Future Food Modern Industry, Xihua University, Chengdu 610039, China. Electronic address:
The effects of high-intensity ultrasound (HIU) on the dispersibility of myofibrillar proteins (MPs) in low-salt medium were investigated. HIU-assisted STPP or TSPP could sharply improve the solubility and dispersibility of MPs (from 38.12 % to 94.
View Article and Find Full Text PDFInt J Mol Sci
January 2025
PhysioLab, University of Florence, 50019 Sesto Fiorentino, Italy.
In maximally Ca-activated demembranated fibres from the mammalian skeletal muscle, the depression of the force by lowering the temperature below the physiological level (~35 °C) is explained by the reduction of force in the myosin motor. Instead, cooling is reported to not affect the force per motor in Ca-activated cardiac trabeculae from the rat ventricle. Here, the mechanism of the cardiac performance depression by cooling is reinvestigated with fast sarcomere-level mechanics.
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