My work focused on characterizing phenotypic defects in mutant C. elegans embryos. The goal of my study was to look at interactions between PAM-1 and known cytoskeletal proteins in attempt to better understand how PAM-1 regulates the actomyosin cytoskeleton—focused on three regulators: moesin, ANI-1 and NMY-2. I used RNA interference (RNAi) to observe phenotypic defects in embryos depleted of a gene of interest. The phenotypes I analyzed occur prior to the first division. I looked specifically at pseudocleavage, asymmetric division, and whether there are blebs (protrusions of the plasma membrane) at the points of ingression during division. The interaction of PAM-1 with each gene separately has been of interest in determining possible defects in localization and function of moesin, ANI-1 and NMY-2. The interaction between PAM-1 and cytoskeletal regulators will enable a better understanding of the proteins regulating cortical dynamics. The experiments were done in both wildtype embryos and pam-1 mutant embryos. I compared normal development to defects presented in embryos depleted of these proteins to understand each protein function and piece together the pathway by which they interact with PAM-1 and regulate the cytoskeleton. As well as looking at phenotypic defects, we looked at the localization of proteins—specifically non-muscle myosin and moesin—in pam-1 mutants to further establish the mechanisms by which PAM-1 organizes these protein networks during anterior-posterior axis polarization.