In vivo roles for Arp2/3 in cortical actin organization during C. elegans gastrulation.


Journal Article

The Arp2/3 complex is important for morphogenesis in various developmental systems, but specific in vivo roles for this complex in cells that move during morphogenesis are not well understood. We have examined cellular roles for Arp2/3 in the Caenorhabditis elegans embryo. In C. elegans, the first morphogenetic movement, gastrulation, is initiated by the internalization of two endodermal precursor cells. These cells undergo a myosin-dependent apical constriction, pulling a ring of six neighboring cells into a gap left behind on the ventral surface of the embryo. In agreement with a previous report, we found that in Arp2/3-depleted C. elegans embryos, membrane blebs form and the endodermal precursor cells fail to fully internalize. We show that these cells are normal with respect to several key requirements for gastrulation: cell cycle timing, cell fate, apicobasal cell polarity and apical accumulation and activation of myosin-II. To further understand the function of Arp2/3 in gastrulation, we examined F-actin dynamics in wild-type embryos. We found that three of the six neighboring cells extend short, dynamic F-actin-rich processes at their apical borders with the internalizing cells. These processes failed to form in embryos that were depleted of Arp2/3 or the apical protein PAR-3. Our results identify an in vivo role for Arp2/3 in the formation of subcellular structures during morphogenesis. The results also suggest a new layer to the model of C. elegans gastrulation: in addition to apical constriction, internalization of the endoderm might involve dynamic Arp2/3-dependent F-actin-rich extensions on one side of a ring of cells.

Full Text

Cited Authors

  • Roh-Johnson, M; Goldstein, B

Published Date

  • November 2009

Published In

Volume / Issue

  • 122 / Pt 21

Start / End Page

  • 3983 - 3993

PubMed ID

  • 19889970

Pubmed Central ID

  • 19889970

Electronic International Standard Serial Number (EISSN)

  • 1477-9137

International Standard Serial Number (ISSN)

  • 0021-9533

Digital Object Identifier (DOI)

  • 10.1242/jcs.057562


  • eng