Female meiosis involves a highly asymmetrical division to form a large secondary oocyte and a small polar body. This process is important for retaining organelles and making a viable embryo. Polo-like kinase I (Plk1) is a serine/threonine kinase which is highly conserved from yeast to human and has been found to be a potent regulator of mitosis and meiosis involved in many cellular roles such as cytokinesis. Plk1 is known to regulate myosin via the activation of RhoA which leads to the contraction of the cleavage furrow in mitotic cells. In this study, it was observed that Plk1 inhibition in late metaphase I oocytes had disrupted cortical actin localisation. N-Wasp, which is an upstream protein in the actin polymerisation pathway, was not able to localise to the cortical region in these oocytes. However, when Plk1 was inhibited in MII eggs, no difference in actin localisation was observed which suggested regulatory differences between actin cap establishment and maintenance. In order to investigate this, MII eggs which had their actin caps depolymerised were treated with Plk1 inhibitor, and were then observed if they could then re-establish their polarised cortex. These eggs were found to have an absence of N-Wasp localisation with a significantly reduced actin presence. In conclusion, it is hypothesised that in meiosis I, Plk1 plays an important role in N-Wasp-mediated cortical actin establishment that complements the role of Plk1 in myosin activation and thereby provides a mechanism for co-ordinating events of cytokinesis.