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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Blotting, Western
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CHO Cells
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Cloning, Molecular
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Cricetinae
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Cystic Fibrosis Transmembrane Conductance Regulator / chemistry
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DNA, Complementary / metabolism
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Endoplasmic Reticulum / enzymology*
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HeLa Cells
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Humans
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Ligases / chemistry*
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Ligases / metabolism*
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Microscopy, Fluorescence
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Molecular Sequence Data
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Protein Structure, Tertiary
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Recombinant Proteins / metabolism
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Saccharomyces cerevisiae Proteins*
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Sequence Homology, Amino Acid
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Time Factors
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Tissue Distribution
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Transfection
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Ubiquitin / metabolism
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Ubiquitin-Protein Ligases*
Substances
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CFTR protein, human
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DNA, Complementary
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Recombinant Proteins
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Saccharomyces cerevisiae Proteins
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Ubiquitin
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Cystic Fibrosis Transmembrane Conductance Regulator
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HRD1 protein, S cerevisiae
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Ubiquitin-Protein Ligases
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Ligases