Interplay among oxidative stress, redox signaling, er stress, autophagy, and protein ubiquitylation in cardiometabolic disorders

Normal function of proteins is essential to all aspects of life. Attaining and maintaining the proper folding of a protein is required for normal functioning of the protein. As the intracellular and extracellular stresses (e.g., oxidative stress) can cause protein malfolding (both misfolding and unfolding) and deployment of a misfolded protein could be catastrophic, the cell has developed an elaborate network of molecular chaperones and targeted protein degradation pathways including the proteasomal degradation pathway and the autophagy to minimize the level and the toxicity of malfolded proteins in the cell. This set of intertwined mechanisms is known as protein quality control (PQC). This chapter focuses on an emerging role of ubiquitylation in regulating PQC-associated protein degradation in the setting of oxidative and endoplasmic reticulum stresses associated with cardiometabolic diseases.