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Current Protein & Peptide Science

Editor-in-Chief

ISSN (Print): 1389-2037
ISSN (Online): 1875-5550

Review Article

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

Author(s): Suzanne J. Randle and Heike Laman*

Volume 18 , Issue 7 , 2017

Page: [715 - 724] Pages: 10

DOI: 10.2174/1389203717666160311121433

Price: $65

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.

Graphical Abstract

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