title: Peroxisomal protein import and ERAD: variations on a common theme.
abstract: Despite their distinct biological functions, there is a surprising similarity between the composition of the machinery that imports proteins into peroxisomes and the machinery that degrades endoplasmic reticulum (ER)-associated proteins. The basis of this similarity lies in the fact that both machineries make use of the same basic mechanistic principle: the tagging of a substrate by monoubiquitylation or polyubiquitylation and its subsequent recognition and ATP-dependent removal from a membrane by ATPases of the ATPases associated with diverse cellular activities (AAA) family of proteins. We propose that the ER-associated protein degradation (ERAD)-like removal of the peroxisomal import receptor is mechanically coupled to protein translocation into the organelle, giving rise to a new concept of export-driven import.
authors.affiliation: Ruhr-Universität Bochum, Medizinische Fakultät, Institut für Physiologische Chemie, Abteilung für Systembiochemie, Universitätsstraße 150, D-44780 Bochum, Germany.
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Schliebs
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Girzalsky
authors.forename: Ralf
authors.initials: R
authors.lastname: Erdmann
mesh_terms: D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D008954:Models, Biological; D020675:Peroxisomes / Q000378:metabolism*; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D021381:Protein Transport / Q000502:physiology*; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology
chemical_list: D029701:Saccharomyces cerevisiae Proteins