title: Proliferation of the endoplasmic reticulum occurs normally in cells that lack a functional unfolded protein response.
abstract: Increased expression of certain ER membrane proteins leads to biogenesis of novel ER membrane arrays. These structures provide models in which to explore the mechanisms by which cells control the size and organization of organelles in response to changing physiological demands. In yeast, elevated levels of HMG-CoA reductase induce ER arrays known as karmellae. Cox and co-workers (1997) discovered that karmellae assembly is toxic to ire1 mutants. These mutants are unable to initiate the unfolded protein response, which enables cells to adjust levels of ER chaperones in response to stresses. We sought to determine whether the karmellae-dependent death of ire1 mutants was due to karmellae assembly or to increased levels of HMG-CoA reductase activity. Unexpectedly, we found that ire1 cells could assemble normal levels of karmellae that were structurally identical to those of wild-type cells. In addition, karmellae assembly did not itself induce the unfolded protein response. Certain ire1 strains produced significant numbers of transformants that were unable to utilize galactose as sole carbon source. These results suggest that the karmellae-dependent death of certain ire1 strains may simply reflect their inability to grow on galactose.
authors.affiliation: University of Washington, Department of Zoology, Seattle, WA 98195-1800, USA.
authors.forename: Lynnelle L
authors.initials: LL
authors.lastname: Larson
authors.forename: Mark L
authors.initials: ML
authors.lastname: Parrish
authors.forename: Ann J
authors.initials: AJ
authors.lastname: Koning
authors.forename: Robin L
authors.initials: RL
authors.lastname: Wright
mesh_terms: D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005656:Fungal Proteins / Q000502:physiology*; D005690:Galactose / Q000378:metabolism; D006903:Hydroxymethylglutaryl CoA Reductases / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D008562:Membrane Glycoproteins / Q000502:physiology; D009154:Mutation; D017510:Protein Folding; D017346:Protein Serine-Threonine Kinases; D029701:Saccharomyces cerevisiae Proteins; D014170:Transformation, Genetic; D014415:Tunicamycin / Q000494:pharmacology; D015003:Yeasts / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure
chemical_list: D005656:Fungal Proteins; D008562:Membrane Glycoproteins; D029701:Saccharomyces cerevisiae Proteins; D014415:Tunicamycin; D006903:Hydroxymethylglutaryl CoA Reductases; C082863:IRE1 protein, S cerevisiae; D017346:Protein Serine-Threonine Kinases; D005690:Galactose