Research Paper Volume 13, Issue 1 pp 77—88
Fbxo7 and Pink1 play a reciprocal role in regulating their protein levels
- 1 Department of Neurology, Fujian Medical University Union Hospital, Fuzhou, China
- 2 Department of Ophthalmology, Fujian Medical University Union Hospital, Fuzhou, China
- 3 Hotchkiss Brain Institute, Department of Clinical Neurosciences, University of Calgary, Calgary T2N 4N1, Alberta, Canada
Received: June 11, 2020 Accepted: October 20, 2020 Published: December 3, 2020https://doi.org/10.18632/aging.202236
How to Cite
Copyright: © 2020 Huang et al. This is an open access article distributed under the terms of the Creative Commons Attribution License (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Pink1, Parkin and Fbxo7, three autosomal recessive familial genes of Parkinson’s disease (PD), have been implicated in mitophagy pathways for quality control and clearance of damaged mitochondria, but the interplay of these three genes still remains unclear. Here we present that Fbxo7 and Pink1 play a reciprocal role in the regulation of their protein levels. Regardless of the genotypes of Fbxo7, the wild type and the PD familial mutants of Fbxo7 stabilize the processed form of Pink1, supporting the prior study that none of the PD familial mutations in Fbxo7 have an effect on the interaction with Pink1. On the other hand, the interaction of Fbxo7 with Bag2 further facilitates its capability to stabilize Pink1. Intriguingly, the stabilization of Fbxo7 by Pink1 is specifically observed in substantial nigra pars compacta but striatum and cerebral cortex. Taken together, our findings support the notion that Fbxo7 as a scaffold protein has a chaperon activity in the stabilization of proteins.