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Published online
doi:10.1083/jcb.200805148
The Journal of Cell Biology, Vol. 184, No. 6, 909-921
The Rockefeller University Press, 0021-9525 $30.00
© Lin et al.
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Article

G{alpha}12/13 regulate epiboly by inhibiting E-cadherin activity and modulating the actin cytoskeleton



Fang Lin1,3, Songhai Chen2, Diane S. Sepich4, Jennifer Ray Panizzi4, Sherry G. Clendenon5, James A. Marrs5, Heidi E. Hamm1, and Lilianna Solnica-Krezel4

1 Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232
2 Department of Pharmacology and 3 Department of Anatomy and Cell Biology, Carver College of Medicine, University of Iowa, Iowa City, IA 52242
4 Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235
5 Department of Medicine, Indiana University Medical Center, Indianapolis, IN 46202

Correspondence to Fang Lin: fang-lin{at}uiowa.edu; Heidi E. Hamm: heidi.hamm{at}vanderbilt.edu; or Lilianna Solnica-Krezel: lilianna.solnica-krezel{at}vanderbilt.edu

Epiboly spreads and thins the blastoderm over the yolk cell during zebrafish gastrulation, and involves coordinated movements of several cell layers. Although recent studies have begun to elucidate the processes that underlie these epibolic movements, the cellular and molecular mechanisms involved remain to be fully defined. Here, we show that gastrulae with altered G{alpha}12/13 signaling display delayed epibolic movement of the deep cells, abnormal movement of dorsal forerunner cells, and dissociation of cells from the blastoderm, phenocopying e-cadherin mutants. Biochemical and genetic studies indicate that G{alpha}12/13 regulate epiboly, in part by associating with the cytoplasmic terminus of E-cadherin, and thereby inhibiting E-cadherin activity and cell adhesion. Furthermore, we demonstrate that G{alpha}12/13 modulate epibolic movements of the enveloping layer by regulating actin cytoskeleton organization through a RhoGEF/Rho-dependent pathway. These results provide the first in vivo evidence that G{alpha}12/13 regulate epiboly through two distinct mechanisms: limiting E-cadherin activity and modulating the organization of the actin cytoskeleton.

Abbreviations used in this paper: C&E, convergence and extension; cdh1, cadherin1; CT, carboxy terminal; CyT, cytoplasmic terminus; dcm, deep cell margin; df, dorsal forerunner; EVL, enveloping layer; GEF, guanine nucleotide exchange factor; GPCR, G protein–coupled receptor; hab, half-baked; LWR, length-to-width ratio; MO, morpholino oligonucleotide; ntl, no tail; WT, wild type; YCL, yolk cytoplasmic layer; YSL, yolk syncytial layer; YSN, yolk syncytial nuclei.

© 2009 Lin et al.
This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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