Published online 31 May 2005. doi:10.1083/jcb.200501104
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 169, Number 5, 777-787
Essential roles of G
12/13 signaling in distinct cell behaviors driving zebrafish convergence and extension gastrulation movements
Fang Lin1,
Diane S. Sepich2,
Songhai Chen1,
Jacek Topczewski2,3,
Chunyue Yin2,
Lilianna Solnica-Krezel2, and
Heidi Hamm1
1 Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232
2 Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235
3 Department of Pediatrics, Northwestern University, Feinberg School of Medicine, Children's Memorial Institute for Education and Research, Chicago, IL 60614
Correspondence to Lilianna Solnica-Krezel: lilianna.solnica-krezel{at}Vanderbilt.edu; or Heidi Hamm: heidi.hamm{at}vanderbilt.edu
G
12/13 have been implicated in numerous cellular processes, however, their roles in vertebrate gastrulation are largely unknown. Here, we show that during zebrafish gastrulation, suppression of both G
12 and G
13 signaling by overexpressing dominant negative proteins and application of antisense morpholino-modified oligonucleotide translation interference disrupted convergence and extension without changing embryonic patterning. Analyses of mesodermal cell behaviors revealed that G
12/13 are required for cell elongation and efficient dorsalward migration during convergence independent of noncanonical Wnt signaling. Furthermore, G
12/13 function cell-autonomously to mediate mediolateral cell elongation underlying intercalation during notochord extension, likely acting in parallel to noncanonical Wnt signaling. These findings provide the first evidence that G
12 and G
13 have overlapping and essential roles in distinct cell behaviors that drive vertebrate gastrulation.
Abbreviations used in this paper: C&E, convergence and extension; dpf, days postfertizilation; GPCR, G proteincoupled receptor; HEK, human embryonic kidney; hpf, hours postfertizilation; LWR, length to width ratio; MO, morpholino-modified oligonucleotide; Rok, Rho kinase; WT, wild-type.

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