title: ER stress: Autophagy induction, inhibition and selection.
abstract: An accumulation of unfolded or misfolded proteins in the endoplasmic reticulum (ER) leads to stress conditions. To mitigate such circumstances, stressed cells activate a homeostatic intracellular signaling network cumulatively called the unfolded protein response (UPR), which orchestrates the recuperation of ER function. Macroautophagy (hereafter autophagy), an intracellular lysosome-mediated bulk degradation pathway for recycling and eliminating wornout proteins, protein aggregates, and damaged organelles, has also emerged as an essential protective mechanism during ER stress. These 2 systems are dynamically interconnected, and recent investigations have revealed that ER stress can either stimulate or inhibit autophagy. However, the stress-associated molecular cues that control the changeover switch between induction and inhibition of autophagy are largely obscure. This review summarizes the crosstalk between ER stress and autophagy and their signaling networks mainly in mammalian-based systems. Additionally, we highlight current knowledge on selective autophagy and its connection to ER stress.
authors.affiliation: a Department of Pharmacology ; Medical School; Chonbuk National University.
authors.forename: Harun-Or
authors.initials: HO
authors.lastname: Rashid
authors.affiliation: a Department of Pharmacology ; Medical School; Chonbuk National University.
authors.forename: Raj Kumar
authors.initials: RK
authors.lastname: Yadav
authors.affiliation: b Department of Dental Pharmacology ; College of Dentistry; Wonkwang University.
authors.forename: Hyung-Ryong
authors.initials: HR
authors.lastname: Kim
authors.affiliation: a Department of Pharmacology ; Medical School; Chonbuk National University.
authors.forename: Han-Jung
authors.initials: HJ
authors.lastname: Chae
keywords: ER stress; autophagy; lysosome; protein aggregates; unfolded protein response