Mechanisms of cell positioning during C. elegans gastrulation.
Cell rearrangements are crucial during development. In this study, we use C. elegans gastrulation as a simple model to investigate the mechanisms of cell positioning. During C. elegans gastrulation, two endodermal precursor cells move from the ventral surface to the center of the embryo, leaving a gap between these ingressing cells and the eggshell. Six neighboring cells converge under the endodermal precursors, filling this gap. Using an in vitro system, we observed that these movements occurred consistently in the absence of the eggshell and the vitelline envelope. We found that movement of the neighbors towards each other is not dependent on chemotactic signaling between these cells. We further found that C. elegans gastrulation requires intact microfilaments, but not microtubules. The primary mechanism of microfilament-based motility does not appear to be through protrusive structures, such as lamellipodia or filopodia. Instead, our results suggest an alternative mechanism. We found that myosin activity is required for gastrulation, that the apical sides of the ingressing cells contract, and that the ingressing cells determine the direction of movement of their neighboring cells. Based on these results, we propose that ingression is driven by an actomyosin-based contraction of the apical side of the ingressing cells, which pulls neighboring cells underneath. We conclude that apical constriction can function to position blastomeres in early embryos, even before anchoring junctions form between cells.
Lee
Jen-Yi
JY
Department of Biology, University of North Carolina, Chapel Hill, NC 27599, USA.
Goldstein
Bob
B
D008841:Actin Cytoskeleton / Q000378:metabolism; D000199:Actins / Q000378:metabolism; D000818:Animals; D019521:Body Patterning; D019086:Bridged Bicyclo Compounds, Heterocyclic / Q000494:pharmacology; D017173:Caenorhabditis elegans / Q000033:anatomy & histology / Q000196:embryology* / Q000502:physiology; D019070:Cell Lineage; D016764:Cell Polarity; D002633:Chemotaxis / Q000502:physiology; D015638:Cytochalasin D / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005775:Gastrula / Q000166:cytology / Q000187:drug effects / Q000502:physiology*; D008164:Luminescent Proteins / Q000378:metabolism; D008954:Models, Biological; D009024:Morphogenesis; D015739:Nocodazole / Q000494:pharmacology; D019384:Nucleic Acid Synthesis Inhibitors / Q000494:pharmacology; D017239:Paclitaxel / Q000494:pharmacology; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D013844:Thiazoles / Q000494:pharmacology; D053778:Thiazolidines
D000199:Actins; D019086:Bridged Bicyclo Compounds, Heterocyclic; D004791:Enzyme Inhibitors; D008164:Luminescent Proteins; D019384:Nucleic Acid Synthesis Inhibitors; D011993:Recombinant Fusion Proteins; D013844:Thiazoles; D053778:Thiazolidines; D015638:Cytochalasin D; C037068:latrunculin B; D017239:Paclitaxel; D015739:Nocodazole