Sec61p is required for ERAD-L: Genetic dissection of the translocation and ERAD-L functions of Sec61P using novel derivatives of CPY

Martin Willer, G. M A Forte, Colin J. Stirling

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Misfolded proteins in the endoplasmic reticulum (ER) are exported to the cytosol for degradation by the proteasome in a process known as ER-associated degradation (ERAD). CPY* is a well characterized ERAD substrate whose degradation is dependent upon the Hrd1 complex. However, although the functions of some of the components of this complex are known, the nature of the protein dislocation channel remains obscure. Sec61p has been suggested as an obvious candidate because of its role as a protein-conducting channel through which polypeptides are initially translocated into the ER. However, it has not yet been possible to functionally dissect any role for Sec61p in dislocation from its essential function in translocation. By changing the translocation properties of a series of novel ERAD substrates, we are able to separate these two events and find that functional Sec61p is essential for the ERAD-L pathway. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.
    Original languageEnglish
    Pages (from-to)33883-33888
    Number of pages5
    JournalJournal of Biological Chemistry
    Volume283
    Issue number49
    DOIs
    Publication statusPublished - 5 Dec 2008

    Fingerprint

    Dive into the research topics of 'Sec61p is required for ERAD-L: Genetic dissection of the translocation and ERAD-L functions of Sec61P using novel derivatives of CPY'. Together they form a unique fingerprint.

    Cite this