Methods for Analyzing eIF2 Kinases and Translational Control in the Unfolded Protein Response
作者： Brian F. Teske , Thomas D. Baird , Ronald C. Wek
DOI: 10.1016/B978-0-12-385114-7.00019-2
关键词: eIF2 、 Eukaryotic translation 、 Unfolded protein response 、 Initiation factor 、 Biochemistry 、 Biology 、 Cell biology 、 Translational regulation 、 Endoplasmic reticulum 、 Protein kinase A 、 Phosphorylation
摘要: Endoplasmic reticulum (ER) stress induces a program of translational and transcriptional regulation, designated the unfolded protein response (UPR), that collectively remedies damage restores ER homeostasis. The kinase PERK facilitates control arm UPR by phosphorylation eIF2, translation initiation factor combines with GTP to escort initiator Met-tRNA(i)(Met) ribosomal machinery during synthesis. Phosphorylation alpha subunit eIF2 on serine-51 inhibits global initiation, which reduces influx nascent polypeptides into overloaded ER. also preferential stress-related mRNAs, such as ATF4 in turn activates transcription genes. In this chapter, we present experimental strategies methods for establishing characterizing gene-specific induced (eIF2α~P) stress. These include assays detection eIF2α~P its target We discuss address whether given condition triggers through PERK, opposed other conditions activating alternative members family. Additionally, descriptions are provided detecting quantifying repression identifying stress-induced translation, described ATF4. Together, these will provide useful molecular "toolkit" study each feature processes invoked
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