In Drosophila oocytes, the pole (germ) plasm, a specialised cytoplasm at the oocyte posterior, contains the maternal RNAs and proteins that are essential for germline and abdominal development. Akira Nakamura and co-workers now describe the role that the Golgi-endosomal protein Mon2 plays in pole plasm anchoring (see p. 2523). Pole plasm assembly begins with the transport of oskar (osk) RNA to the oocyte posterior where it is translated. Osk then stimulates endocytosis, which promotes an actin remodelling event that is essential for pole plasm anchoring. The researchers report that Mon2 interacts with Cappuccino and Spire, actin nucleators involved in osk RNA localisation in the oocyte, and promotes the accumulation of the small GTPase Rho1 at the oocyte posterior. In oocytes lacking Mon2, actin remodelling does not occur in response to Osk-induced endocytosis and pole plasm components are not correctly anchored. The researchers propose, therefore, that Mon2 is a scaffold that links Osk-induced vesicles with actin regulators to anchor the pole plasm to the oocyte cortex.