Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains.
Mammalian cells acquire tolerance against multiple stressors through the high-level expression of stress-responsible genes. We have previously demonstrated that protein-disulfide isomerase (PDI) together with ubiquilin are up-regulated in response to hypoxia/brain ischemia, and play critical roles in resistance to these damages. We show here that ubiquilin interacts preferentially with poly-ubiquitin ... chains and 19S proteasome subunits. Taken together, these results suggest that ubiquitin could serve as an adaptor protein that both interacts with PDI and mediates the delivery of poly-ubiquitylated proteins to the proteasome in the cytosol in the vicinity of the endoplasmic reticulum membrane.
Mesh Terms:
Carrier Proteins, Cell Cycle Proteins, Cell Line, Cell Line, Tumor, Cysteine Endopeptidases, Gene Deletion, Humans, Multienzyme Complexes, Polyubiquitin, Proteasome Endopeptidase Complex, Protein Binding, Protein Structure, Tertiary, Recombinant Proteins, Repressor Proteins, Saccharomyces cerevisiae Proteins, Transfection, Two-Hybrid System Techniques, Ubiquitin, Yeasts
Carrier Proteins, Cell Cycle Proteins, Cell Line, Cell Line, Tumor, Cysteine Endopeptidases, Gene Deletion, Humans, Multienzyme Complexes, Polyubiquitin, Proteasome Endopeptidase Complex, Protein Binding, Protein Structure, Tertiary, Recombinant Proteins, Repressor Proteins, Saccharomyces cerevisiae Proteins, Transfection, Two-Hybrid System Techniques, Ubiquitin, Yeasts
FEBS Lett.
Date: May. 21, 2004
PubMed ID: 15147878
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