Abstract:
:Endoplasmic reticulum (ER) stress sensors use a related luminal domain to monitor the unfolded protein load and convey the signal to downstream effectors, signaling an unfolded protein response (UPR) that maintains compartment-specific protein folding homeostasis. Surprisingly, perturbation of cellular lipid composition also activates the UPR, with important consequences in obesity and diabetes. However, it is unclear if direct sensing of the lipid perturbation contributes to UPR activation. We found that mutant mammalian ER stress sensors, IRE1α and PERK, lacking their luminal unfolded protein stress-sensing domain, nonetheless retained responsiveness to increased lipid saturation. Lipid saturation-mediated activation in cells required an ER-spanning transmembrane domain and was positively regulated in vitro by acyl-chain saturation in reconstituted liposomes. These observations suggest that direct sensing of the lipid composition of the ER membrane contributes to the UPR.
journal_name
Proc Natl Acad Sci U S Aauthors
Volmer R,van der Ploeg K,Ron Ddoi
10.1073/pnas.1217611110subject
Has Abstractpub_date
2013-03-19 00:00:00pages
4628-33issue
12eissn
0027-8424issn
1091-6490pii
1217611110journal_volume
110pub_type
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