Androgen receptor (AR) is able to promote stress-induced cell death independently of its transcription activity in androgen-independent prostate cancer cells. Yet, the underlying mechanism is incompletely understood. Here we report that stress-induced proteasomal degradation of AR contributes to its pro-death activity. Upon exposure to ultraviolet light and staurosporine, AR underwent proteasomal degradation. Blockade of AR degradation significantly suppressed stresses-induced apoptosis in androgen-independent prostate cancer cells. Ectopic expression of the AR N-terminal domain (AR-N), which lacks DNA- and ligand-binding abilities, led to cell death without any additional death stimuli. Truncation analysis revealed that AR-N contains several sub-domains that regulate the pro-death activity of AR, specifically the first 105 amino acids which function as a minimal pro-death domain acting upstream of caspases. The pro-apoptotic activity of AR-N terminal fragments was suppressed by ectopic expression of Bc1-2 or caspase inhibitors. Thus, our results reveal a novel mechanism by which AR promotes stress-induced cell death in androgen-independent prostate cancer cells.