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| Investigating the Role of the Arp2/3 Complex during C. elegans Gastrulation |
| Presentation Time: Sunday, 12:00 noon - 3:00 p.m. |
| M. Roh, B. Goldstein; University of North Carolina, Chapel Hill, NC |
| Presentation Number: 242 |
| Poster Board Number: B189 |
| Gastrulation is a crucial process during embryonic morphogenesis that shapes the body plan of organisms. Regulated cell movements are critical for gastrulation, and these movements require intricate coordination of cytoskeletal components. Although gastrulation is imperative for development, the molecular mechanisms underlying gastrulation cell movements in C. elegans are still unknown. Cellular actin architecture is remodeled based on signalling events and upstream actin regulators in diverse cell types. One such regulator is the Arp2/3 complex. This complex acts to nucleate new actin filaments off existing actin filaments and, thus, affects overall actin organization. In C. elegans, gastrulation is initiated by the ingression of two endodermal precursor cells, Ea and Ep. The apical region of the E cells constrict, thereby pulling in the neighbouring cells such that they cover the E cells as the E cells ingress into the interior (Lee and Goldstein, 2003). In addition, myosin is also activated in the apical region of the E cells, as indicated by an accumulation of phosphorylated myosin light chain (Lee et al., submitted). Depleting C. elegans Arp-related proteins, ARX-2 and ARX-3, result in gastrulation defects. In these embryos, gastrulation is not initiated and the E cells divide on the surface of the embryo (Severson et al., 2002). Currently, the effects of Arp2/3 components on the actin cytoskeleton and/or polarity of the cells, particularly Ea and Ep, are unknown. However, our preliminary evidence suggests that active myosin still accumulates in the apical region of the E cells, but the E-cells still fail to ingress (D. Marston, pers. comm.). Using a combination of live and fixed microscopy, we are determining whether the polarity is altered in Ea and Ep. We are also determining which cells require Arp2/3 function through blastomere isolation techniques, and we are analyzing the effects of depleting Arp2/3 components on actin architecture. |
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