title: Checkpoints in ER-associated degradation: excuse me, which way to the proteasome?
abstract: The failure of secreted proteins to fold results in their retrotranslocation from the endoplasmic reticulum (ER) and degradation by the proteasome in a process called "ER-associated degradation" (ERAD). Two recent studies indicate that ERAD substrates are targeted to different pathways depending on the topology of the substrate and the subcellular location of the misfolded domain.
authors.affiliation: Department of Biological Sciences, University of Pittsburgh, 274 Crawford Hall, 4249 Fifth Avenue, Pittsburgh, PA 15260, USA.
authors.forename: Annette
authors.initials: A
authors.lastname: Ahner
authors.forename: Jeffrey L
authors.initials: JL
authors.lastname: Brodsky
mesh_terms: D000818:Animals; D003593:Cytoplasm / Q000378:metabolism; D003600:Cytosol / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism; D006801:Humans; D008954:Models, Biological; D018832:Molecular Chaperones / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism*; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D012441:Saccharomyces cerevisiae / Q000378:metabolism
chemical_list: D005656:Fungal Proteins; D018832:Molecular Chaperones; D046988:Proteasome Endopeptidase Complex