title: Differential fates of invertase mutants in the yeast endoplasmic reticulum.
abstract: A number of proteins have been identified as substrates for endoplasmic reticulum (ER)-associated protein degradation (ERAD) and we describe here a new model substrate with which to study this process. Two secretion-defective forms of yeast invertase that accumulated in the ER to greatly different levels were examined: Suc2-538p levels were low, while Suc2-533p was present in high amounts. Because Suc2-533p and Suc2-538p mRNA levels were comparable, we examined whether Suc2-538p was targeted for degradation. Both mutant polypeptide levels were unaffected in a yeast strain deficient in vacuolar protease activity and, additionally, we showed that Suc2-538p was stabilized in ERAD-deficient strains, demonstrating that Suc2-538p was a substrate for ERAD.
authors.affiliation: Biology Department, University of Nevada, Reno, NV 89557, USA. mccracke@cmb.unr.edu
authors.forename: A A
authors.initials: AA
authors.lastname: McCracken
authors.forename: E D
authors.initials: ED
authors.lastname: Werner
authors.forename: M J
authors.initials: MJ
authors.lastname: Powell
authors.forename: K B
authors.initials: KB
authors.lastname: Kruse
authors.forename: J L
authors.initials: JL
authors.lastname: Brodsky
mesh_terms: D000818:Animals; D002645:Chickens; D004721:Endoplasmic Reticulum / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D007136:Immunoglobulins / Q000276:immunology; D009154:Mutation; D043324:beta-Fructofuranosidase
chemical_list: C016512:IgY; D007136:Immunoglobulins; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase