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Afadin and Zyxin contribute to coupling between cell junctions and contracting actomyosin networks during apical constriction

ABSTRACT: One of the most common cell shape changes driving morphogenesis in diverse animals is the constriction of the apical surface. Apical constriction depends on contraction of an actomyosin network in the apical cell cortex, but such actomyosin networks have been shown to undergo continual, conveyor belt-like contractions even before the shrinking of an apical surface begins. This finding suggests that apical constriction is not necessarily triggered by the contraction of actomyosin networks, but rather by unidentified, temporally-regulated mechanical linking of actomyosin to the cell junctions. Here, we used C. elegans gastrulation as a model to identify proteins that contribute to such linkage. We found that α-catenin and β-catenin initially failed to move centripetally with contracting cortical actomyosin networks, suggesting that linkage is regulated between cadherin-catenin complexes and actomyosin. We used a proteomic approach to identify AFD-1/afadin and transcriptomics to identify ZYX-1/zyxin as contributors to C. elegans gastrulation. We found that a zyxin family of LIM domain proteins have transcripts that become enriched in multiple cells just before they undergo apical constriction. Using a new, semi-automated image analysis tool, we found that AFD-1/afadin and ZYX-1/zyxin both contribute to cell-cell junctions’ centripetal movement along contracting actomyosin networks. These results identify two key proteins as important for actomyosin networks to effectively pull cell-cell junctions inward during apical constriction. The transcriptional upregulation of zyxin/ZYX-1 in specific cells points to one way that developmental patterning spatiotemporally regulates cell biological mechanisms in vivo. Because afadin- and zyxin-family proteins contribute to membrane-cytoskeleton linkage in other systems, we anticipate that their roles in regulating apical constriction in this manner may be conserved.

ORGANISM(S): Caenorhabditis elegans

PROVIDER: GSE205061 | GEO | 2022/06/30

REPOSITORIES: GEO

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Project description:Development and homeostasis of blood vessels critically depend on the regulation of endothelial cell-cell junctions. Perturbations in cell-cell junction organization and function results in developmental defects and vascular pathologies including chronic inflammation, edema and atherosclerosis. Although many aspects of blood vessel formation and homeostasis depend on cell-cell junctions, the molecular mechanisms that regulate their dynamic rearrangement are not fully understood. The VEcad-catenin complex, which constitute the molecular basis of the adherens junctions (AJ), is connected to the actin cytoskeleton and its function is regulated by cytoskeletal contraction and actin-driven plasma membrane protrusions. Junction-associated intermitted lamellipodia (JAIL) are small actin-driven protrusions at cell-cell junctions controlled by the actin related protein 2/3 (Arp2/3)-complex that contribute to the regulation of cell-cell junctions. JAIL drive VEcad dynamics within the cell-cell junction thereby being critical for monolayer integrity, cell migration and angiogenesis. The molecular mechanisms regulating JAIL during vessel development are not completely understood. Coronin 1B (Coro1B) is an actin binding protein that controls actin networks at classical lamellipodia via both Arp2/3 complex and cofilin-mediated pathways. The role of Coro1B in endothelial cell (ECs) is not fully understood. In this study we demonstrate that Coro1B is a novel component and regulator of cell-cell junctions in ECs. Immunofluorescence studies show that Coro1B colocalizes with VEcad at cell-cell junctions in monolayers of ECs. Live-cell imaging reveal that Coro1B is recruited to, and operated at, actin-driven membrane protrusions at the cell-cell junctions. Coro1B recruitment to cell-cell junctions is regulated by cytoskeleton tension. By analyzing the Coro1B interactome, we identify integrin linked kinase (ILK) as new Coro1B-associated protein. Coro1B colocalizes with α-parvin, an interactor of ILK, at the leading edge of lamellipodia protrusions. Finally, functional experiments reveal that depletion of Coro1B causes defects in actin cytoskeleton and cell-cell junctions. In matrigel vessel network assays, depletion of Coro1B results in reduced network complexity, vessel number and vessel length. Together, our findings point towards a critical role for Coro1B in the dynamic remodeling of endothelial cell-cell junction and the assembly of vessel network.

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Afadin and Zyxin contribute to coupling between cell junctions and contracting actomyosin networks during apical constriction

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