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The mechanism by which this occurs has not been elucidated completely. Using a proteotoxic yeast model of Huntington's disease, we show that the deletion of <jats:italic>Ire1<\/jats:italic> led to lower protein aggregation at longer time points. The rate of protein degradation was higher in \u0394<jats:italic>Ire1<\/jats:italic> cells. We monitored the two major protein degradation mechanisms in the cell. The increase in expression of <jats:italic>Rpn4<\/jats:italic>, coding for the transcription factor controlling proteasome biogenesis, was higher in \u0394<jats:italic>Ire1<\/jats:italic> cells. The chymotrypsin\u2010like proteasomal activity was also significantly enhanced in these cells at later time points of aggregation. The gene and protein expression levels of the autophagy gene <jats:italic>Atg8<\/jats:italic> were higher in \u0394<jats:italic>Ire1<\/jats:italic> than in wild\u2010type cells. Significant increase in autophagy flux was also seen in \u0394<jats:italic>Ire1<\/jats:italic> cells at later time points of aggregation. The results suggest that the deletion of <jats:italic>Ire1<\/jats:italic> activates UPR\u2010independent arms of the proteostasis network, especially under conditions of aggravated stress. 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