This is the author accepted manuscript. It is currently under an indefinite embargo pending publication by Bentham Science. ; Fbxo7/PARK15 has well-defined roles, acting as part of a Skp1-Cul1-F box protein (SCF)-type E3 ubiquitin ligase and also has SCF-independent activities. Mutations within FBXO7 have been found to cause an early-onset Parkinson?s disease, and these are found within or near to its functional domains, including its F-box domain (FBD), its proline rich region (PRR), and its ubiquitin-like domain (Ubl). We highlight recent advances in our understanding of Fbxo7 function in Parkinson?s disease, with respect to these mutations and where they occur in the Fbxo7 protein. We hypothesize that many of Fbxo7 functions contribute to its role in PD pathogenesis.