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Vol. 17, Issue 7, 3095-3107, July 2006
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Division of Biological Sciences, Section of Molecular Biology, University of California, San Diego, La Jolla, CA, 92093-0377
Submitted January 24, 2006;
Revised March 27, 2006;
Accepted April 26, 2006
Monitoring Editor: Benjamin Glick
The unfolded protein response (UPR) regulates the protein-folding capacity of the endoplasmic reticulum (ER) according to cellular demand. In mammalian cells, three ER transmembrane components, IRE1, PERK, and ATF6, initiate distinct UPR signaling branches. We show that these UPR components display distinct sensitivities toward different forms of ER stress. ER stress induced by ER Ca2+ release in particular revealed fundamental differences in the properties of UPR signaling branches. Compared with the rapid response of both IRE1 and PERK to ER stress induced by thapsigargin, an ER Ca2+ ATPase inhibitor, the response of ATF6 was markedly delayed. These studies are the first side-by-side comparisons of UPR signaling branch activation and reveal intrinsic features of UPR stress sensor activation in response to alternate forms of ER stress. As such, they provide initial groundwork toward understanding how ER stress sensors can confer different responses and how optimal UPR responses are achieved in physiological settings.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
Address correspondence to: Maho Niwa ( niwa{at}ucsd.edu)
Abbreviations used: DTT, dithiothreitol; ER, endoplasmic reticulum; Tg, thapsigargin; Tm, tunicamycin; UPR, unfolded protein response.
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