title: Structure and Function of Fbxo7/PARK15 in Parkinson's Disease.
abstract: Fbxo7/PARK15 has well-defined roles, acting as part of a Skp1-Cul1-F box protein (SCF)- type E3 ubiquitin ligase and also having 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 ubiquitinlike 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.
authors.affiliation: Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom.
authors.forename: Suzanne J
authors.initials: SJ
authors.lastname: Randle
authors.affiliation: Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom.
authors.forename: Heike
authors.initials: H
authors.lastname: Laman
mesh_terms: D000818:Animals; D004331:Drosophila melanogaster / Q000235:genetics / Q000378:metabolism; D044783:F-Box Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D015870:Gene Expression; D006801:Humans; D009154:Mutation; D009474:Neurons / Q000378:metabolism / Q000473:pathology; D010300:Parkinson Disease / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D000072417:Protein Domains; D044843:SKP Cullin F-Box Protein Ligases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D013329:Structure-Activity Relationship; D054875:Ubiquitination
chemical_list: D044783:F-Box Proteins; C489149:FBXO7 protein, human; D044843:SKP Cullin F-Box Protein Ligases
keywords: E3 ligase; F-box protein; Fbxo7/PARK15; Parkinson's disease; SCF-ligase; mitophagy; ubiquitin