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A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1.

Authors:
Nadav E, Shmueli A, Barr H, Gonen H, Ciechanover A, Reiss Y
Affiliation:
Journal:
Biochemical and biophysical research communications

Abstract

The yeast hHrd1 is a ubiquitin-protein ligase (E3) involved in ER-associated degradation. It was originally identified by genetic methods as an E3 of the yeast cholesterol biosynthetic enzyme HMG-CoA reductase (HMGR). We report the identification and cloning of a human homologue of Hrd1 (hHrd1). Immunofluorescence imaging confirms that the endogenous hHrd1 resides in the ER and in vitro assay demonstrates that it has a ubiquitin-ligase activity. However, the homology between the human and yeast Hrd1 is limited to the N-terminal domain of the proteins, and hHrd1 does not appear to be involved in the degradation of mammalian HMGR.

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