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unfolded protein responses with or without unfolded proteins展开的蛋白质反应有或没有展开的蛋白质
Cells 2012, 1, 926-950; doi:10.3390/cells1040926
OPEN ACCESS
cells
ISSN 2073-4409
/journal/cells
Review
Unfolded Protein Responses With or Without Unfolded Proteins?
Erik L. Snapp
Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, 1300 Morris
Park Avenue, Bronx, NY 10461, USA; E-Mail: erik-lee.snapp@; Tel.: +718-430-2967;
Fax: +718-430-8996
Received: 17 September 2012; in revised form: 15 October 2012 / Accepted: 22 October 2012 /
Published: 1 November 2012
Abstract: The endoplasmic reticulum (ER) is the site of secretory protein biogenesis. The
ER quality control (QC) machinery, including chaperones, ensures the correct folding of
secretory proteins. Mutant proteins and environmental stresses can overwhelm the
available QC machinery. To prevent and resolve accumulation of misfolded secretory
proteins in the ER, cells have evolved integral membrane sensors that orchestrate the
Unfolded Protein Response (UPR). The sensors, Ire1p in yeast and IRE1, ATF6, and
PERK in metazoans, bind the luminal ER chaperone BiP during homeostasis. As unfolded
secretory proteins accumulate in the ER lumen, BiP releases, and the sensors activate. The
mechanisms of activation and attenuation of the UPR sensors have exhibited unexpected
complexity. A growing body of data supports a model in which Ire1p, and potentially
IRE1, directly bind unf
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