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Formin-mediated actin polymerization at endothelial junctions is required for vessel lumen formation and stabilization
journal contribution
posted on 2023-06-08, 21:11 authored by Li-Kun Phng, Véronique Gebala, Katie Bentley, Andy PhilippidesAndy Philippides, Andrin Wacker, Thomas Mathivet, Loïc Sauteur, Fabio Stanchi, Heinz-Georg Belting, Markus Affolter, Holger GerhardtDuring 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.
History
Publication status
- Published
Journal
Developmental CellISSN
1534-5807Publisher
ElsevierExternal DOI
Issue
1Volume
32Page range
123-132Department affiliated with
- Informatics Publications
Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2015-06-19Usage metrics
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