Targeted protein destabilization reveals an estrogen-mediated ER stress response.
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ABSTRACT:
SUBMITTER: Raina K
PROVIDER: S-EPMC4324732 | biostudies-literature | 2014 Nov
REPOSITORIES: biostudies-literature
Publications
Targeted protein destabilization reveals an estrogen-mediated ER stress response.
Raina Kanak K Noblin Devin J DJ Serebrenik Yevgeniy V YV Adams Alison A Zhao Connie C Crews Craig M CM
Nature chemical biology 20140921 11
Accumulation of unfolded proteins within the endoplasmic reticulum (ER) of eukaryotic cells leads to an unfolded protein response (UPR) that either restores homeostasis or commits the cells to apoptosis. Tools traditionally used to study the UPR are proapoptotic and thus confound analysis of long-term cellular responses to ER stress. Here, we describe an ER-localized HaloTag (ERHT) protein that can be conditionally destabilized using a small-molecule hydrophobic tag (HyT36). Treatment of ERHT-ex ...[more]
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