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.
Keywords: Fbxo7/PARK15, F-box protein, SCF-ligase, ubiquitin, E3 ligase, Parkinson’s disease, mitophagy.
Current Protein & Peptide Science
Title:Structure and Function of Fbxo7/PARK15 in Parkinson's Disease
Volume: 18 Issue: 7
Author(s): Suzanne J. Randle and Heike Laman*
Affiliation:
- Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP,United Kingdom
Keywords: Fbxo7/PARK15, F-box protein, SCF-ligase, ubiquitin, E3 ligase, Parkinson’s disease, mitophagy.
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.
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Cite this article as:
Randle J. Suzanne and Laman Heike*, Structure and Function of Fbxo7/PARK15 in Parkinson's Disease, Current Protein & Peptide Science 2017; 18 (7) . https://dx.doi.org/10.2174/1389203717666160311121433
DOI https://dx.doi.org/10.2174/1389203717666160311121433 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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