Journal
MOLECULAR BIOTECHNOLOGY
Volume 34, Issue 2, Pages 279-290Publisher
HUMANA PRESS INC
DOI: 10.1385/MB:34:2:279
Keywords
endoplasmic reticulum; molecular chaperone; recombinant protein production; signal transduction; unfolded protein response
Funding
- Biotechnology and Biological Sciences Research Council [BB/C513418/1] Funding Source: Medline
- Biotechnology and Biological Sciences Research Council [BB/C513418/1] Funding Source: researchfish
Ask authors/readers for more resources
The unfolded protein response (UPR) is a signal transduction network activated by inhibition of protein folding in the endoplasmic reticulum (ER). The UPR coordinates adaptive responses to this stress situation, including induction of ER resident molecular chaperone and protein foldase expression to increase the protein folding capacity of the ER, induction of phospholipid synthesis, attenuation of general translation, and upregulation of ER-associated degradation to decrease the unfolded protein load of the ER, and an antioxidant response. Upon severe or prolonged ER stress the UPR induces apoptosis to eliminate unhealthy cells from an organism or a population. In this review, I will summarize our current knowledge about signal transduction pathways involved in transducing the unfolded protein signal from the ER to the nucleus or the cytosol.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available