Abstract
Cellular forces sculpt organisms during development, while misregulation of cellular mechanics can promote disease. Here, we investigate how the actomyosin scaffold protein anillin contributes to epithelial mechanics in Xenopus laevis embryos. Increased mechanosensitive recruitment of vinculin to cell-cell junctions when anillin is overexpressed suggested that anillin promotes junctional tension. However, junctional laser ablation unexpectedly showed that junctions recoil faster when anillin is depleted and slower when anillin is overexpressed. Unifying these findings, we demonstrate that anillin regulates medial-apical actomyosin. Medial-apical laser ablation supports the conclusion that that tensile forces are stored across the apical surface of epithelial cells, and anillin promotes the tensile forces stored in this network. Finally, we show that anillin's effects on cellular mechanics impact tissue-wide mechanics. These results reveal anillin as a key regulator of epithelial mechanics and lay the groundwork for future studies on how anillin may contribute to mechanical events in development and disease.
Highlights
During development, an organism takes its shape by generating forces and establishing mechanical properties at the cellular level (Davidson, 2012)
We show that anillin promotes a contractile medial-apical actomyosin network, which produces tensile forces in individual cells that are transmitted between cells via cell–cell junctions to promote tissue stiffness
Anillin increases junctional vinculin recruitment but reduces recoil of junction vertices after laser ablation. Since anillin can both promote and limit contractility at the cytokinetic contractile ring (Piekny and Glotzer, 2008; Manukyan et al, 2015; Descovich et al, 2018), and anillin localizes to cell–cell junctions where it maintains F-actin, myosin II, and proper active RhoA distribution (Reyes et al, 2014), we sought to test whether anillin affects junctional tension
Summary
An organism takes its shape by generating forces and establishing mechanical properties at the cellular level (Davidson, 2012). Anillin anchors the contractile ring to the plasma membrane by binding to actomyosin through its N-terminal myosin- and F-actin-binding domains and to lipids through its C-terminal C2 and PH domains (Straight et al, 2005; Piekny and Glotzer, 2008; Liu et al, 2012; Sun et al, 2015). Anillin can both enhance and limit contractility during cytokinesis through binding directly to active RhoA as well as several proteins that positively or negatively
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