Int. J. Mol. Sci. 2013, 14(3), 6454-6466; doi:10.3390/ijms14036454
Review

UPR Signal Activation by Luminal Sensor Domains

Marta Carraraemail, Filippo Prischiemail and Maruf M. U. Ali* email
Department of Life Sciences, Centre for Structural Biology, Imperial College London, London SW7 2AZ, UK
* Author to whom correspondence should be addressed.
Received: 30 January 2013; in revised form: 15 March 2013 / Accepted: 18 March 2013 / Published: 21 March 2013
(This article belongs to the Special Issue Signalling Molecules and Signal Transduction in Cells)
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Abstract: The unfolded protein response (UPR) is a cell-signaling system that detects the accumulation of unfolded protein within the endoplasmic reticulum (ER) and initiates a number of cellular responses to restore ER homeostasis. The presence of unfolded protein is detected by the ER-luminal sensor domains of the three UPR-transducer proteins IRE1, PERK, and ATF6, which then propagate the signal to the cytosol. In this review, we discuss the various mechanisms of action that have been proposed on how the sensor domains detect the presence of unfolded protein to activate downstream UPR signaling.
Keywords: unfolded protein response; ER-stress; signaling

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Cite This Article

MDPI and ACS Style

Carrara, M.; Prischi, F.; Ali, M.M.U. UPR Signal Activation by Luminal Sensor Domains. Int. J. Mol. Sci. 2013, 14, 6454-6466.

AMA Style

Carrara M, Prischi F, Ali MMU. UPR Signal Activation by Luminal Sensor Domains. International Journal of Molecular Sciences. 2013; 14(3):6454-6466.

Chicago/Turabian Style

Carrara, Marta; Prischi, Filippo; Ali, Maruf M.U. 2013. "UPR Signal Activation by Luminal Sensor Domains." Int. J. Mol. Sci. 14, no. 3: 6454-6466.

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