Bundles of actin filaments and molecular motors of the myosin family are a common subcellular organizational motif. Typically, such bundles are under contractile stress resulting from interactions between the filaments and the motors. This holds in particular for contractile rings that appear in the late stages of cell division in animal cells and that cleave the mother into two daughter cells. It was recently shown that myosin organizes into regularly spaced clusters along rings in mammalian cells, whereas myosin clusters in fission yeast travel along the perimeter of actomyosin rings [Wollrab et al., Nat. Commun. 7, 11860 (2016)2041-172310.1038/ncomms11860]. A mechanism based on the association of the structurally polar actin filaments into bipolar structures was shown to provide a common explanation for both observations. Here, we analyze the dynamics of this mechanism in detail. We find a rich phase diagram depending on the actomyosin interaction strength and the stability of the bipolar structures. The system can notably organize into traveling waves. Furthermore, we identify the nature of the bifurcations connecting the various patterns as parameters are changed. Finally, we report experimental patterns observed in cytokinetic rings in fission yeast and link them to solutions of our dynamic equations. Our analysis highlights the possible role played by local polarity sorting of actin filaments for the dynamics and functionality of actomyosin networks.
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http://dx.doi.org/10.1103/PhysRevE.98.012413 | DOI Listing |
J Nanobiotechnology
January 2025
School of Medicine, Shanghai University, Shanghai, 200444, China.
Biochips are widely applied to manipulate the geometrical morphology of stem cells in recent years. Patterned antenna-like pseudopodia are also probed to explore the influence of pseudopodia formation on gene delivery and expression on biochips. However, how the antenna-like pseudopodia affect gene transfection is unsettled and the underlying trafficking mechanism of exogenous genes in engineered single cells is not announced.
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January 2025
Department of Biological Sciences and Bioengineering, Indian Institute of Technology Kanpur, Kanpur 208016, Uttar Pradesh, India; Mehta Family Center for Engineering in Medicine (MFCEM), Indian Institute of Technology Kanpur, Kanpur 208016, Uttar Pradesh, India. Electronic address:
Telencephalic hemisphere formation is a complex and precisely timed process, which begins in the chick forebrain with an invagination in the middle of the roof plate. However, the factor(s) that determine the position/site of invagination in the roof plate remain to be elucidated. In this study, we have demonstrated that as development proceeds, a region of lower thickness appears in the middle of the roof plate, which marks the position where the invagination begins.
View Article and Find Full Text PDFPlant Physiol
January 2025
State Key Laboratory of Tree Genetics and Breeding, College of Biological Sciences and Technology, Beijing Forestry University, Beijing 100083, China.
In plants, cytoskeletal proteins assemble into dynamic polymers that play numerous roles in diverse fundamental cellular processes, including endocytosis, vesicle trafficking, and the spatial distribution of organelles and protein complexes. Plant elicitor peptides (Peps) are damage/danger-associated molecular patterns (DAMPs) that are perceived by the receptor-like kinases PEP RECEPTOR 1 (PEPR1) and PEPR2 to enhance innate immunity and inhibit root growth in Arabidopsis (Arabidopsis thaliana). To date, however, there is little evidence that the actin cytoskeleton of the host cell participates in DAMP-induced innate immunity.
View Article and Find Full Text PDFActa Biochim Biophys Sin (Shanghai)
January 2025
Annexins are a family of multifunctional calcium-dependent and phospholipid-binding proteins that are widely distributed in the plant kingdom. They have a highly conserved evolutionary history that dates back to single-celled protists. Plant annexins, as soluble proteins, can flexibly bind to endomembranes and plasma membranes, exhibiting unique calcium-dependent and calcium-independent characteristics.
View Article and Find Full Text PDFAdv Exp Med Biol
January 2025
Cancer Research UK Scotland Centre (Edinburgh), Institute of Genetics & Cancer, University of Edinburgh, Edinburgh, UK.
E-cadherin is a transmembrane protein and central component of adherens junctions (AJs). The extracellular domain of E-cadherin forms homotypic interactions with E-cadherin on adjacent cells, facilitating the formation of cell-cell adhesions, known as AJs, between neighbouring cells. The intracellular domain of E-cadherin interacts with α-, β- and p120-catenins, linking the AJs to the actin cytoskeleton.
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