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Dev Cell. 2015 Jan 12;32(1):123-32. doi: 10.1016/j.devcel.2014.11.017.

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

Author information

1
Vascular Patterning Laboratory, Vesalius Research Center, VIB, Department of Oncology, KU Leuven, Herestraat 49, 3000 Leuven, Belgium.
2
Vascular Biology Laboratory, London Research Institute, Cancer Research UK, London WC2A 3LY, UK.
3
Computational Biology Laboratory, Center for Vascular Biology Research, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA.
4
Centre for Computational Neuroscience and Robotics, Department of Informatics, University of Sussex, Brighton BN1 9QJ, UK.
5
Biozentrum der Universität Basel, Klingelbergstrasse 50/70, 4056 Basel, Switzerland.
6
Vascular Patterning Laboratory, Vesalius Research Center, VIB, Department of Oncology, KU Leuven, Herestraat 49, 3000 Leuven, Belgium; Vascular Biology Laboratory, London Research Institute, Cancer Research UK, London WC2A 3LY, UK. Electronic address: holger.gerhardt@mdc-berlin.de.

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.

PMID:
25584798
DOI:
10.1016/j.devcel.2014.11.017
[Indexed for MEDLINE]
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