| Literature DB >> 23906563 |
Nilesh Chitnis1, Dariusz Pytel, J Alan Diehl.
Abstract
The endoplasmic reticulum (ER) senses both extracellular and intracellular stresses that can disrupt its ability to facilitate the maturation of proteins destined for secretory pathways. The accumulation of misfolded proteins within the ER triggers an adaptive signaling pathway coined the unfolded protein response (UPR). UPR activation contributes to cell adaptation by reducing the rate of protein translation while increasing the synthesis of chaperones. Although we have gained considerable insight into the mechanisms that regulate gene expression and certain aspects of protein translation, the contribution of miRNAs to UPR-dependent activities has only recently been investigated. Here we highlight recent insights into the contribution of miRNAs to UPR-dependent cellular adaptive responses. 2013 Elsevier Ltd. All rights reservedEntities:
Keywords: ER stress; activating transcription factor 6 (ATF6); apoptosis; inositol-regulated enzyme 1α (IRE1α); microRNA; protein kinase RNA-like endoplasmic reticulum kinase (PERK); unfolded protein response (UPR)
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Year: 2013 PMID: 23906563 PMCID: PMC4056666 DOI: 10.1016/j.tibs.2013.06.012
Source DB: PubMed Journal: Trends Biochem Sci ISSN: 0968-0004 Impact factor: 13.807