Der1p, a protein required for degradation of malfolded soluble proteins of the endoplasmic reticulum: topology and Der1-like proteins

Authors

  • Reiner Hitt,

    1. Institut für Biochemie, Universität Stuttgart, Pfaffenwaldring 55, 70569 Stuttgart, Germany
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  • Dieter H. Wolf

    Corresponding author
    1. Institut für Biochemie, Universität Stuttgart, Pfaffenwaldring 55, 70569 Stuttgart, Germany
      *Corresponding author. Tel.: +49-711-685-4390; fax: +49-711-685-4392, E-mail address: dieter.wolf@po.uni-stuttgart.de
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*Corresponding author. Tel.: +49-711-685-4390; fax: +49-711-685-4392, E-mail address: dieter.wolf@po.uni-stuttgart.de

Abstract

The endoplasmic reticulum (ER) contains a highly effective protein quality control system eliminating malfolded proteins by a mechanism called ER-associated protein degradation (ERAD). Here, we unravel the topology of Der1p, a previously identified component of the ERAD system. Der1p contains four transmembrane domains, its N- and C-terminus protrude into the cytoplasm and contribute to its function. Additionally, we describe a yeast homologue of Der1p, Dfm1p, which does not seem to be involved in ERAD. In contrast, a Caenorhabditis elegans orthologue of Der1p, R151.6, is capable of complementing der1-defective phenotypes in yeast.

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