Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8469600 | European Journal of Cell Biology | 2018 | 22 Pages |
Abstract
IRE1α (Inositol Requiring kinase Enzyme 1 alpha), a transmembrane protein localized to the endoplasmic reticulum (ER) is a master regulator of the unfolded protein response (UPR) pathway. The fate determining steps during ER stress-induced apoptosis are greatly attributed to IRE1α's endoribonuclease and kinase activities. Apart from its role as a chief executioner in ER stress, recent studies have shown that upon activation in the presence or absence of ER stress, IRE1α executes multiple cellular processes such as differentiation, immune response, progression and repression of the cell cycle. Besides its crucial role in protein misfolding, the versatile contributions of IRE1α in other cellular functions are greatly unknown. In this review, we have discussed the structural conservation of IRE1 among eukaryotes, the mechanisms underlying its activation and the recent understandings of the non-apoptotic functions of IRE1 other than ER stress-induced cell death.
Keywords
TNF receptor associated factor 2NLSGRP78Bcl2TRAF2DR5XBP1IRE1UPREndoribonucleaseBcl-2 interacting mediator of cell deathbZIPATFmTORERADHac1basic leucine zipper domainErdj4JnkBiPc-Jun N-terminal kinaseROSAktCHOPRIDDnuclear localization signalendoplasmic reticulumactivating transcription factorB cell lymphoma 2BIMmammalian target of rapamycinUnfolded protein responseX-box binding protein 1Binding immunoglobulin ProteinCCAAT-enhancer-binding protein homologous proteinglucose regulated protein 78Reactive oxygen speciesdeath receptor 5
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Authors
Ahmad Abdullah, Palaniyandi Ravanan,