Increased interaction between endoplasmic reticulum and mitochondria following sleep deprivation.

ABSTRACT:

Background

Prolonged cellular activity may overload cell function, leading to high rates of protein synthesis and accumulation of misfolded or unassembled proteins, which cause endoplasmic reticulum (ER) stress and activate the unfolded protein response (UPR) to re-establish normal protein homeostasis. Previous molecular work has demonstrated that sleep deprivation (SD) leads to ER stress in neurons, with a number of ER-specific proteins being upregulated to maintain optimal cellular proteostasis. It is still not clear which cellular processes activated by sleep deprivation lead to ER- stress, but increased cellular metabolism, higher request for protein synthesis, and over production of oxygen radicals have been proposed as potential contributing factors. Here, we investigate the

SUBMITTER: Aboufares El Alaoui A 

PROVIDER: S-EPMC9814192 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature