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1.
Fig. 2

Fig. 2. From: Intracellular Death Platform Steps-In: Targeting Prostate Tumors Via Endoplasmic Reticulum (ER) Apoptosis.

ER stress-induced apoptotic signal transduction. This cartoon highlights how hyperactive ER stress stimuli sensed by IRE1, ATF6, and PERKmight result in apoptosis induction. A cross-talk between the mitochondrial, death receptor and ER stress apoptotic pathways may contribute to apoptosis mediated by chemical agents or by the accumulation of unfolded proteins.

Steven R. Schwarze, et al. Prostate. ;68(15):1615-1623.
2.
Fig. 1

Fig. 1. From: Intracellular Death Platform Steps-In: Targeting Prostate Tumors Via Endoplasmic Reticulum (ER) Apoptosis.

Sensing ER stress and subsequent signal transduction. Three main ER-resident transmembrane proteins (IRE1, ATF6, and PERK) in mammals can act as ER stress sensors. When ER stress is sensed, GRP78 becomes disassociated with the proteins allowing their activation. PERK responds to the ER stress by decreasing global translation. Signaling through IRE1 and ATF6 results in a transcription response to the ER stress mediatedbyXBP-1 and ATF6. These genes can act alone or in concert to increase protein folding machinery and initiate proteasomal degradation ofER-resident proteins. The full role for unspliced and spliced forms of XBP1 (uXBP1 and sXBP1) in confronting the ER stress is not yet understood.

Steven R. Schwarze, et al. Prostate. ;68(15):1615-1623.

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