Nuclear migration is a critical aspect of many developmental and cellular processes including fertilization, cell polarization, and differentiation. Disruptions of the nuclear envelope migration machinery lead to a variety of diseases including Hutchinson-Gilford Progeria Syndrome, Emery-Dreifuss Muscular Dystrophy, cancer and autism. For nuclear migration to occur, a bridge termed the LINC complex (for linker of nucleoskeleton and cytoskeleton), forms across the nuclear envelope to connect nuclear lamins to microtubule motors. In C. elegans, the LINC complex utilized for moving nuclei consists of the KASH protein, UNC-83 in the outer nuclear membrane and the SUN protein UNC-84 in the inner nuclear membrane. We have previously shown that UNC-83 recruits microtubule motors to the surface of the nucleus and UNC-84 interacts with the lamin LMN-1 to disperse forces throughout the nucleus. P-cell nuclear migration occurs during mid L1. The P-cell nucleus is approximately 3-4 µm in diameter, but must migrate through a 150 nm space between the body wall muscle and the cuticle of the worm. We hypothesize that dramatic cytoskeletal and nucleoskeletal rearrangements are necessary for nuclear migration through constricted spaces. We are investigating the roles of the cytoskeleton and nucleoskeleton during this nuclear migration event by visualizing these components in vivo. We aim to characterize the interacting roles of microtubule and actin pathways, as well as identify the role of the nuclear lamina in P-cell nuclear migration. Our data suggest a role for dynein as the primary microtubule motor functioning to move nuclei during P cell nuclear migration, while kinesin plays a more minor role. This is opposite to the roles of kinesin and dynein in embryonic hypodermal nuclear migrations. Additionally, a genetic screen for enhancers of unc-84 implicates the actin cytoskeleton in P-cell nuclear migration. We are therefore investigating the dynamics of the actin network in P-cell development by live cell imaging of tagged actin binding proteins. We hypothesize nuclear lamina breakdown is necessary for nuclear reorganization to squeeze into the constricted space and used CRISPR/Cas9 to make a functional, GFP-tagged LMN-1. Our working model postulates that the nuclear lamina is remodeled to allow nuclei to squeeze through tight spaces, dynein provides the major force for P-cell nuclear migration, and kinesin and actin cables within the cell assist in nuclear migration.