Tau Protein Linked to Mitochondrial Reverse Electron Transport in Preclinical Models
The results of a preclinical study demonstrated that phosphorylated tau enters mitochondria and initiates a vicious cycle of pathological events that trigger reverse electron transport. The post Tau Protein Linked to Mitochondrial Reverse Electron Transport in Preclinical Models appeared first on GEN - Genetic Engineering and Biotechnology News .
Researchers at Stanford University and the University of California, San Francisco have discovered a new mechanism linking tau protein to neurodegenerative diseases. In neurons, tau protein is usually involved in stabilizing microtubules, which are essential for proper cell function. However, when hyperphosphorylated, tau can enter mitochondria and disrupt the electron transport chain (ETC), triggering a pathological cycle of events.
This newly identified reverse electron transport (RET) process produces reactive oxygen species (ROS), leading to inflammation and damage to proteins. The study, published in Neuron, reveals that RET may serve as a common pathogenic mechanism in tauopathies, including Alzheimer's, Parkinson's, and Huntington's diseases. The findings suggest that targeting RET could be a novel therapeutic approach to counteract the detrimental effects of tau abnormalities in these diseases.
Written by urgent.news from GEN Biotechnology's reporting — not their text. Machine-written — may contain errors; check the original before relying on it.
