Vps4 is a AAA ATPase that regulates events leading to membrane constriction and scission within three fundamental biological processes: the terminal stages of cytokinesis; the biogenesis of multivesicular-bodies within the endosomal protein sorting pathway, and the acquisition of a plasma membrane coat by a subset of nascently-formed enveloped virus during exocytosis from infected cells. Specifically, Vps4 catalyses the removal of protein components of the ESCRT-III complex from lipid membranes – the penultimate step to membrane fission – and this functionality is hijacked by numerous enveloped viruses including HIV, Hepatitis B and C, Herpes simplex and Ebola in the late stages of viral budding. Functional knockdown of Vps4 has been shown to confer protection against enveloped virus infection in live mice and inhibit virus budding in cultured cells confirming that the virus infection pathway is entirely dependent of this enzyme and making it a therapeutic target of high interest. Despite some early successes, the structure of the oligomeric Vps4 apoenzyme remains a topic of fierce scientific debate. This study aims to analyze the structure of Vps4 oligomeric protein complexes and identify the molecular basis of interaction between the enzyme and components of the ESCRT pathway by using a combination of biochemical, molecular biological, biophysical and molecular structure determination techniques.