Mitochondrial and Clearance Impairment in p.D620N VPS35 Patient-Derived Neurons.

ABSTRACT:

Background

VPS35 is part of the retromer complex and is responsible for the trafficking and recycling of proteins implicated in autophagy and lysosomal degradation, but also takes part in the degradation of mitochondrial proteins via mitochondria-derived vesicles. The p.D620N mutation of VPS35 causes an autosomal-dominant form of Parkinson's disease (PD), clinically representing typical PD.

Objective

Most of the studies on p.D620N VPS35 were performed on human tumor cell lines, rodent models overexpressing mutant VPS35, or in patient-derived fibroblasts. Here, based on identified target proteins, we investigated the implication of mutant VPS35 in autophagy, lysosomal degradation, and mitochondrial function in induced pluripotent stem cell-derived neurons from a patient harbo

SUBMITTER: Hanss Z 

PROVIDER: S-EPMC8048506 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature