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Papers In Press, published online ahead of print October 11, 2001
Centre for Cancer Therapeutics, Ottawa Regional Cancer Centre, Ottawa, Ontario K1H 8L6
Corresponding Author: Doug.Gray{at}orcc.on.ca
There is convincing evidence from studies with yeast that a functional ubiquitin/proteasome pathway is required to degrade misfolded or oxidatively damaged proteins, but for technical reasons it has been difficult to perform comparable studies in mammalian cells. To investigate the possibility that the ubiquitin/proteasome pathway is cytoprotective for mammalian cells we have introduced epitope-tagged wild-type ubiquitin or dominant negative mutant versions of ubiquitin into mouse HT4 neuroblastoma cells. Cells expressing mutant versions of ubiquitin were found to be sensitive to cadmium, an agent that causes oxidative damage to cellular components, and to canavanine, an amino acid analog that generates misfolded proteins. The greatest sensitivity to canavanine was observed in cells expressing a mutant version of ubiquitin unable to support the formation of K48 linkages. Substrates of the proteasome were found to accumulate in these cells, suggesting a general deficit in proteolysis. Our data suggest that defects in the ubiquitin-mediated proteolytic system predispose mammalian cells to the toxic effects of abnormal protein.
J. Biol. Chem, 10.1074/jbc.M109023200
Submitted on September 18, 2001
Revised on October 11, 2001
Accepted on October 10, 2001
Sensitivity of mammalian cells expressing mutant ubiquitin to protein damaging agents
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