CHOP is a multifunctional transcription factor in the ER stress response.
TLDR
CCAAT-enhancer-binding protein homologous protein (CHOP) is induced by ER stress and mediates apoptosis and the multifunctional roles of CHOP in the ER stress response are discussed below.Abstract:
The accumulation of unfolded proteins in the endoplasmic reticulum (ER) induces ER stress. To restore ER homeostasis, cells possess a highly specific ER quality-control system called the unfold protein response (UPR). In the case of prolonged ER stress or UPR malfunction, apoptosis signalling is activated. This ER stress-induced apoptosis has been implicated in the pathogenesis of several conformational diseases. CCAAT-enhancer-binding protein homologous protein (CHOP) is induced by ER stress and mediates apoptosis. Recent studies by the Gotoh group have shown that the CHOP pathway is also involved in ER stress-induced cytokine production in macrophages. The multifunctional roles of CHOP in the ER stress response are discussed below.read more
Citations
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References
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Journal ArticleDOI
Roles of CHOP/GADD153 in endoplasmic reticulum stress.
TL;DR: The current understanding of the roles of C/EBP homologous protein (CHOP) and GADD153 in ER stress-mediated apoptosis and in diseases including diabetes, brain ischemia and neurodegenerative disease are summarized.
Journal ArticleDOI
Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
Anne Bertolotti,Yuhong Zhang,Linda M. Hendershot,Linda M. Hendershot,Heather P. Harding,David Ron +5 more
TL;DR: In this article, the lumenal domains of transmembrane protein kinases (PERK and IRE1) were found to be functionally interchangeable in mediating an ER stress response and that in unstressed cells, both L1 and L2 domains formed a stable complex with the ER chaperone BiP.
Dynamic interaction of BiP and ER stress transducers in the unfolded
TL;DR: It is shown that the lumenal domains of these two proteins are functionally interchangeable in mediating an ER stress response and that, in unstressed cells, both lumenAL domains form a stable complex with the ER chaperone BiP.
Journal ArticleDOI
Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress.
Ira Tabas,David Ron +1 more
TL;DR: The molecular mechanisms linking ER stress to apoptosis are the topic of this review, with emphases on relevance to pathophysiology and integration and complementation among the various apoptotic pathways induced by ER stress.
Journal ArticleDOI
Non-canonical inflammasome activation targets caspase-11
Nobuhiko Kayagaki,Søren Warming,Mohamed Lamkanfi,Lieselotte Vande Walle,Salina Louie,Jennifer Dong,Kim Newton,Yan Qu,Jinfeng Liu,Sherry Heldens,Juan Zhang,Wyne P. Lee,Merone Roose-Girma,Vishva M. Dixit +13 more
TL;DR: It is shown, with C57BL/6 Casp11 gene-targeted mice, that caspase-11 is critical for casp enzyme-1 activation and IL-1β production in macrophages infected with Escherichia coli, Citrobacter rodentium or Vibrio cholerae, and a unique pro-inflammatory role for casingase- 11 in the innate immune response to clinically significant bacterial infections is highlighted.
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