title: The Gp78 ubiquitin ligase: probing endoplasmic reticulum complexity.
abstract: The endoplasmic reticulum (ER) has been classically divided, based on electron microscopy analysis, into parallel ribosome-studded rough ER sheets and a tubular smooth ER network. Recent studies have identified molecular constituents of the ER, the reticulons and DP1, that drive ER tubule formation and whose expression determines expression of ER sheets and tubules and thereby rough and smooth ER. However, segregation of the ER into only two domains remains simplistic and multiple functionally distinct ER domains necessarily exist. In this review, we will discuss the sub-organization of the ER in different domains focusing on the localization and role of the gp78 ubiquitin ligase in the mitochondria-associated smooth ER and on the evidence for a quality control ERAD domain.
authors: Department of Cellular and Physiological Sciences, Life Sciences Institute, University of British Columbia, Vancouver, BC, V6T 1Z3, Canada.
authors: Pascal
authors: P
authors: St Pierre
authors: Ivan R
authors: IR
authors: Nabi
mesh_terms: D000818:Animals; D018871:Endoplasmic Reticulum, Smooth / Q000378:metabolism* / Q000648:ultrastructure; D060746:Endoplasmic Reticulum-Associated Degradation / Q000502:physiology*; D006801:Humans; D008928:Mitochondria / Q000378:metabolism; D060285:Receptors, Autocrine Motility Factor / Q000378:metabolism*
chemical_list: C555000:AMFR protein, human; D060285:Receptors, Autocrine Motility Factor