Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Biochem. 2009 Dec;146(6):743-50. doi: 10.1093/jb/mvp166. Epub 2009 Oct 27.

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

Author information

  • 1Department of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa-Oiwake, Sakyo-ku, Kyoto 606-8502, Japan. kazu.mori@bio.mbox.media.kyoto-u.ac.jp

Abstract

The accumulation of unfolded proteins in the endoplasmic reticulum (ER) under ER stress conditions activates a series of homoeostatic responses collectively termed the unfolded protein response (UPR). The UPR is unique in which the molecular mechanisms it uses to transmit signals from the ER lumen to the nucleus are completely different to those used for signalling 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, for example, one in Saccharomyces cerevisiae, two in Caenorhabditis elegans and Drosophila 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 signalling pathways in yeast, worm, fly and mammalian cells. I also discuss how they have evolved to counteract ER stress effectively.

PMID:
19861400
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for HighWire
    Loading ...
    Write to the Help Desk