Document Detail


Structural basis of the unfolded protein response.
MedLine Citation:
PMID:  23057742     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
The unfolded protein response (UPR) is a network of intracellular signaling pathways that maintain the protein-folding capacity of the endoplasmic reticulum (ER) in eukaryotic cells. Dedicated molecular sensors embedded in the ER membrane detect incompletely folded or unfolded proteins in the ER lumen and activate a transcriptional program that increases the abundance of the ER according to need. In metazoans the UPR additionally regulates translation and thus relieves unfolded protein load by globally reducing protein synthesis. If homeostasis in the ER cannot be reestablished, the metazoan UPR switches from the prosurvival to the apoptotic mode. The UPR involves a complex, coordinated action of many genes that is controlled by one ER-embedded sensor, Ire1, in yeasts, and three sensors, Ire1, PERK, and ATF6, in higher eukaryotes, including human. We discuss the emerging molecular understanding of the UPR and focus on the structural biology of Ire1 and PERK, the two recently crystallized UPR sensors.
Authors:
Alexei Korennykh; Peter Walter
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Annual review of cell and developmental biology     Volume:  28     ISSN:  1530-8995     ISO Abbreviation:  Annu. Rev. Cell Dev. Biol.     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-10-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9600627     Medline TA:  Annu Rev Cell Dev Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  251-77     Citation Subset:  IM    
Affiliation:
Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544; email: akorenny@princeton.edu.
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