Stimulation of N-linked glycosylation and lipid-linked oligosaccharide synthesis by stress responses in metazoan cells.
Endoplasmic reticulum (ER) stress responses comprising the unfolded protein response (UPR) are activated by conditions that disrupt folding and assembly of proteins inside the ER lumenal compartment. Conditions known to be proximal triggers of the UPR include saturation of chaperones with misfolded protein, redox imbalance, disruption of Ca2+ levels, interference with N-linked glycosylation, and failure to dispose of terminally misfolded proteins. Potentially, ER stress responses can reprogram cells to correct all of these problems and thereby restore ER function to normal. This article will review literature on stimulation of N-linked glycosylation by ER stress responses, focusing on metazoan systems. The mechanisms involved will be contrasted with those mediating stimulation of N-linked glycosylation by cytoplasmic stress responses. This information will interest readers who study the biological roles of stress responses, the functions of N-linked glycans, and potential strategies for treatment of genetic disorders of N-linked glycosylation.
Lehrman
Mark A
MA
Department of Pharmacology, UT-Southwestern Medical Center, Dallas, TX 75390-9041, USA. mark.lehrman@utsouthwestern.edu
D000222:Adaptation, Physiological; D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006003:Glycogen / Q000378:metabolism; D006031:Glycosylation; D008070:Lipopolysaccharides / Q000096:biosynthesis*; D008954:Models, Biological; D011134:Polysaccharides / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology
D008070:Lipopolysaccharides; D011134:Polysaccharides; C023023:lipid-linked oligosaccharides; D006003:Glycogen