Formin-mediated actin polymerization at endothelial junctions is required for vessel lumen formation and stabilization

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Item Type:	Article
Title:	Formin-mediated actin polymerization at endothelial junctions is required for vessel lumen formation and stabilization
Creators Name:	Phng, L.K., Gebala, V., Bentley, K., Philippides, A., Wacker, A., Mathivet, T., Sauteur, L., Stanchi, F., Belting, H.G., Affolter, M. and Gerhardt, H.
Abstract:	During blood vessel formation, endothelial cells (ECs) establish cell-cell junctions and rearrange to form multicellular tubes. Here, we show that during lumen formation, the actin nucleator and elongation factor, formin-like 3 (fmnl3), localizes to EC junctions, where filamentous actin (F-actin) cables assemble. Fluorescent actin reporters and fluorescence recovery after photobleaching experiments in zebrafish embryos identified a pool of dynamic F-actin with high turnover at EC junctions in vessels. Knockdown of fmnl3 expression, chemical inhibition of formin function, and expression of dominant-negative fmnl3 revealed that formin activity maintains a stable F-actin content at EC junctions by continual polymerization of F-actin cables. Reduced actin polymerization leads to destabilized endothelial junctions and consequently to failure in blood vessel lumenization and lumen instability. Our findings highlight the importance of formin activity in blood vessel morphogenesis.
Keywords:	Actin Cytoskeleton, Actins, Adherens Junctions, Antisense Oligonucleotides, Membrane Proteins, Morpholinos, Nonmammalian Embryo, Physiologic Neovascularization, Polymerization, Signal Transduction, Vascular Endothelium, Zebrafish Proteins, Animals, Zebrafish
Source:	Developmental Cell
ISSN:	1534-5807
Publisher:	Cell Press / Elsevier
Volume:	32
Number:	1
Page Range:	123-132
Date:	12 January 2015
Official Publication:	https://doi.org/10.1016/j.devcel.2014.11.017
PubMed:	View item in PubMed

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