title: Protein degradation and the stress response.
abstract: Environmental stresses are manifold and so are the responses they elicit. This is particularly true for higher eukaryotes where various tissues and cell types are differentially affected by the insult. Type and scope of the stress response can therefore differ greatly among cell types. Given the importance of the ubiquitin proteasome system (UPS) for most cellular processes, it comes as no surprise that the UPR plays a pivotal role in counteracting the effects of stressors. Here we outline contributions of the UPS to stress sensing, signaling, and response pathways. We make no claim to comprehensiveness but choose selected examples to illustrate concepts and mechanisms by which protein modification with ubiquitin and proteasomal degradation of key regulators ensures cellular integrity during stress situations.
authors.affiliation: University of California Irvine, Department of Biological Chemistry, College of Medicine, 240D Med Sci I, Irvine, CA 92697-1700, USA. kflick@uci.edu
authors.forename: Karin
authors.initials: K
authors.lastname: Flick
authors.forename: Peter
authors.initials: P
authors.lastname: Kaiser
mesh_terms: D000818:Animals; D015687:Cell Hypoxia; D006801:Humans; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D059748:Proteolysis; D013312:Stress, Physiological; D054875:Ubiquitination
chemical_list: D011506:Proteins; D046988:Proteasome Endopeptidase Complex