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Journal of Biochemistry Advance Access first published online on October 27, 2009
This version published online on October 30, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp166
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

JB Minireview

Signaling pathways in the unfolded protein response: development from yeast to mammals

Kazutoshi Mori

Department of Biophysics, Graduate School of Science, Kyoto University Kitashirakawa-Oiwake, Sakyo-ku, Kyoto 606-8502, Japan Phone: 81-75-753-4067, Fax: 81-75-753-3718 E-mail: kazu.mori{at}bio.mbox.media.kyoto-u.ac.jp

To whom correspondence should be addressed: Kazutoshi Mori Department of Biophysics, Graduate School of Science, Kyoto University Kitashirakawa-Oiwake, Sakyo-ku, Kyoto 606-8502, Japan Phone: 81-75-753-4067, Fax: 81-75-753-3718 E-mail: kazu.mori{at}bio.mbox.media.kyoto-u.ac.jp

Received September 29, 2009; Accepted October 5, 2009


  Abstract

The accumulation of unfolded proteins in the endoplasmic reticulum (ER) under ER stress conditions activates a series of homeostatic responses collectively termed the unfolded protein response (UPR). The UPR is unique in that the molecular mechanisms it uses to transmit signals from the ER lumen to the nucleus are completely different to those used for signaling from the plasma membrane. An ER stress signal is sensed and transmitted across the membrane by a transmembrane protein(s) in the ER. Interestingly, the number of such functional sensors/transducers ubiquitously expressed has increased with evolution, namely one in S. cerevisiae, two in C. elegans and D. melanogaster, and three in mammals. Accordingly, mammalian cells are able to cope with ER stress in a more sophisticated manner. Here, I summarize the mechanisms and activation consequences of UPR signaling pathways in yeast, worm, fly and mammalian cells. I also discuss how they have evolved to counteract ER stress effectively

Key Words: endoplasmic reticulum, phase shift, protein degradation, protein folding, quality control


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