Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing
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Autophagy-Related Proteins
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Cell Cycle Proteins*
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Cell Line
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Cell Line, Tumor
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Cysteine Endopeptidases / metabolism*
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Gene Deletion
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Humans
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Multienzyme Complexes / metabolism*
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Polyubiquitin / metabolism
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Proteasome Endopeptidase Complex
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Protein Binding
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Protein Structure, Tertiary
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RNA-Binding Proteins
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Repressor Proteins / metabolism
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Saccharomyces cerevisiae Proteins
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Transfection
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Two-Hybrid System Techniques
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Ubiquitin / metabolism*
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Yeasts / genetics
Substances
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Adaptor Proteins, Signal Transducing
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Autophagy-Related Proteins
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Carrier Proteins
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Cell Cycle Proteins
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Multienzyme Complexes
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PSMD4 protein, human
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RNA-Binding Proteins
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RPN10 protein, S cerevisiae
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Recombinant Proteins
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Repressor Proteins
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Saccharomyces cerevisiae Proteins
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UBQLN1 protein, human
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Ubiquitin
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Polyubiquitin
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex