title: The unfolded protein response--a stress signaling pathway of the endoplasmic reticulum.
abstract: The endoplasmic reticulum (ER) is a factory for folding and maturation of newly synthesized transmembrane and secretory proteins. The ER provides stringent quality control systems to ensure that only correctly folded proteins exit the ER and unfolded or misfolded proteins are retained and ultimately degraded. A number of biochemical and physiological stimuli can change ER homeostasis, impose stress to the ER, and subsequently lead to accumulation of unfolded or misfolded proteins in the ER lumen. The ER has evolved stress response signaling pathways collectively called the unfolded protein response (UPR) to cope with the accumulation of unfolded or misfolded proteins. This review summarizes our understanding of the UPR signaling developed in the recent years.
authors.affiliation: Howard Hughes Medical Institute, The University of Michigan Medical Center, 1150 W. Medical Center Drive, Ann Arbor, MI 48109, USA.
authors.forename: Xiaohua
authors.initials: X
authors.lastname: Shen
authors.forename: Kezhong
authors.initials: K
authors.lastname: Zhang
authors.forename: Randal J
authors.initials: RJ
authors.lastname: Kaufman
mesh_terms: D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006801:Humans; D017510:Protein Folding; D015398:Signal Transduction / Q000502:physiology*; D013312:Stress, Physiological / Q000378:metabolism*