Abstract:
:The accumulation of misfolded proteins in the endoplasmic reticulum (ER) activates the Unfolded Protein Response (UPR(ER)) to restore ER homeostasis. The AAA(+) ATPase p97/CDC-48 plays key roles in ER stress by promoting both ER protein degradation and transcription of UPR(ER) genes. Although the mechanisms associated with protein degradation are now well established, the molecular events involved in the regulation of gene transcription by p97/CDC-48 remain unclear. Using a reporter-based genome-wide RNAi screen in combination with quantitative proteomic analysis in Caenorhabditis elegans, we have identified RUVB-2, a AAA(+) ATPase, as a novel repressor of a subset of UPR(ER) genes. We show that degradation of RUVB-2 by CDC-48 enhances expression of ER stress response genes through an XBP1-dependent mechanism. The functional interplay between CDC-48 and RUVB-2 in controlling transcription of select UPR(ER) genes appears conserved in human cells. Together, these results describe a novel role for p97/CDC-48, whereby its role in protein degradation is integrated with its role in regulating expression of ER stress response genes.
journal_name
EMBO Repjournal_title
EMBO reportsauthors
Marza E,Taouji S,Barroso K,Raymond AA,Guignard L,Bonneu M,Pallares-Lupon N,Dupuy JW,Fernandez-Zapico ME,Rosenbaum J,Palladino F,Dupuy D,Chevet Edoi
10.15252/embr.201439123subject
Has Abstractpub_date
2015-03-01 00:00:00pages
332-40issue
3eissn
1469-221Xissn
1469-3178pii
embr.201439123journal_volume
16pub_type
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