Randle Suzanne J, Laman Heike
Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom.
Curr Protein Pept Sci. 2017;18(7):715-724. doi: 10.2174/1389203717666160311121433.
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.
Fbxo7/PARK15具有明确的作用，它作为Skp1-Cul1-F盒蛋白（SCF）型E3泛素连接酶的一部分发挥作用，同时也具有不依赖于SCF的活性。已发现FBXO7内的突变会导致早发性帕金森病，这些突变位于其功能域内或附近，包括其F盒结构域（FBD）、富含脯氨酸区域（PRR）和类泛素结构域（Ubl）。我们着重介绍了在理解Fbxo7在帕金森病中的功能方面的最新进展，涉及这些突变及其在Fbxo7蛋白中的位置。我们推测Fbxo7的许多功能都有助于其在帕金森病发病机制中的作用。
