Related Experiment Video
Updated: Feb 3, 2026

Mitochondria and Endoplasmic Reticulum Imaging by Correlative Light and Volume Electron Microscopy
Published on: July 20, 2019
Alpha-Synuclein Toxicity on Protein Quality Control, Mitochondria and Endoplasmic Reticulum
Thaiany Quevedo Melo1,2, Sjef J C V M Copray2, Merari F R Ferrari3
1Departamento de Genética e Biologia Evolutiva, Instituto de Biociencias, Universidade de Sao Paulo, Rua do Matao, 277, Cidade Universitaria, 05508-090, Sao Paulo, SP, Brazil.
Abstract:
Parkinson's disease (PD) is characterized by the presence of insoluble protein clusters containing α-synuclein. Impairment of mitochondria, endoplasmic reticulum, autophagy and intracellular trafficking proper function has been suggested to be caused by α-synuclein toxicity, which is also associated with the higher levels of ROS found in the aged brain and in PD. Oxidative stress leads to protein oligomerization and aggregation that impair autophagy and mitochondrial dynamics leading to a vicious cycle of organelles damage and neurodegeneration. In this review we focused on the role of α-synuclein dysfunction as a cellular stressor that impairs mitochondria, endoplasmic reticulum, autophagy and cellular dynamics culminating with dopaminergic depletion and the pathogenesis of PD.
Related Concept Videos
Endoplasmic Reticulum
The Endoplasmic Reticulum
Directing Proteins to the Rough Endoplasmic Reticulum
Smooth Endoplasmic Reticulum
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...
Quality Control
Quality control helps track data, visualize trends, and identify variations, making it easier to detect deviations that may affect the accuracy of an analysis. One way to do this is by generating a quality control chart, which...
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

