title: GRP94 in ER quality control and stress responses.
abstract: A system of endoplasmic reticulum (ER) chaperones has evolved to optimize the output of properly folded secretory and membrane proteins. An important player in this network is Glucose Regulated Protein 94 (GRP94). Over the last decade, new structural and functional data have begun to delineate the unique characteristics of GRP94 and have solidified its importance in ER quality control pathways. This review describes our current understanding of GRP94 and the four ways in which it contributes to the ER quality control: (1) chaperoning the folding of proteins; (2) interacting with other components of the ER protein folding machinery; (3) storing calcium; and (4) assisting in the targeting of malfolded proteins to ER-associated degradation (ERAD).
authors.affiliation: Division of Cell Pathology, Department of Pathology and Lab Medicine, The Children's Hospital of Philadelphia and the University of Pennsylvania, 3615 Civic Center Blvd., Philadelphia, PA 19104, USA.
authors.forename: Davide
authors.initials: D
authors.lastname: Eletto
authors.forename: Devin
authors.initials: D
authors.lastname: Dersh
authors.forename: Yair
authors.initials: Y
authors.lastname: Argon
mesh_terms: D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism* / Q000502:physiology*; D018840:HSP70 Heat-Shock Proteins; D008565:Membrane Proteins / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism
chemical_list: D018840:HSP70 Heat-Shock Proteins; D008565:Membrane Proteins; D018832:Molecular Chaperones; D011506:Proteins; C018551:glucose-regulated proteins