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Vol. 11, Issue 5, 1697-1708, May 2000
University of California San Diego, Department of Biology, La
Jolla, California 92093
Work from several laboratories has indicated that many different
proteins are subject to endoplasmic reticulum (ER) degradation by a
common ER-associated machinery. This machinery includes ER membrane
proteins Hrd1p/Der3p and Hrd3p and the ER-associated ubiquitin-conjugating enzymes Ubc7p and Ubc6p. The wide variety of substrates for this degradation pathway has led to the reasonable hypothesis that the HRD (Hmg CoA reductase
degradation) gene-encoded proteins are generally involved in ER protein
degradation in eukaryotes. We have tested this model by directly
comparing the HRD dependency of the ER-associated
degradation for various ER membrane proteins. Our data indicated that
the role of HRD genes in protein degradation, even in
this highly defined subset of proteins, can vary from absolute
dependence to complete independence. Thus, ER-associated degradation
can occur by mechanisms that do not involve Hrd1p or Hrd3p, despite
their apparently broad envelope of substrates. These data favor models
in which the HRD gene-encoded proteins function as
specificity factors, such as ubiquitin ligases, rather than as factors
involved in common aspects of ER degradation.
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