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Structure and Function of Fbxo7/PARK15 in Parkinson's Disease.

Accepted version
Peer-reviewed

Repository DOI


Type

Article

Change log

Authors

Randle, Suzanne J 

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.

Description

Keywords

E3 ligase, F-box protein, Fbxo7/PARK15, Parkinson's disease, SCF-ligase, mitophagy, ubiquitin, Animals, Drosophila melanogaster, F-Box Proteins, Gene Expression, Humans, Mutation, Neurons, Parkinson Disease, Protein Domains, SKP Cullin F-Box Protein Ligases, Structure-Activity Relationship, Ubiquitination

Journal Title

Curr Protein Pept Sci

Conference Name

Journal ISSN

1389-2037
1875-5550

Volume Title

18

Publisher

Bentham Science Publishers Ltd.
Sponsorship
Biotechnology and Biological Sciences Research Council (BB/J007846/1)