The molecular mechanism and functional diversity of UPR signaling sensor IRE1

The endoplasmic reticulum is primarily responsible for protein folding and maturation. However, the organelle is subject to varied stress conditions from time to time, which lead to the activation of a signaling program known as the Unfolded Protein Response (UPR) pathway. This pathway, upon sensing...

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Vydané v:Life sciences (1973) Ročník 265; s. 118740
Hlavní autori: Bashir, Samirul, Banday, Mariam, Qadri, Ozaira, Bashir, Arif, Hilal, Nazia, Nida-i-Fatima, Rader, Stephen, Fazili, Khalid Majid
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: Netherlands Elsevier Inc 15.01.2021
Elsevier BV
Predmet:
Animals
Apoptosis
Cell Nucleus - metabolism
Cytoplasm
Divergent cell fates
DNA-Binding Proteins - metabolism
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Endoplasmic Reticulum Stress
Endoribonucleases - metabolism
Enzymatic activity
Enzymes
ER-stress
Folding
functional diversity
Homeostasis
Humans
Inositol
Inositol-requiring enzyme 1(IRE1)
Kinases
Membrane proteins
Pleiotropy
Protein Folding
Protein-Serine-Threonine Kinases - metabolism
Proteins
Regulated IRE1 Dependent Decay (RIDD)
Ribonuclease
ribonucleases
Signal Transduction
Signaling
Splicing
Substrate Specificity
Substrates
Transcription Factors - metabolism
Unfolded Protein Response
Unfolded Protein Response (UPR)
X-Box Binding Protein 1 - metabolism
X-box protein 1 (Xbp1)
Yeast
yeasts
Unfolded Protein Response (UPR)
X-box protein 1 (Xbp1)
Divergent cell fates
ER-stress
Inositol-requiring enzyme 1(IRE1)
Regulated IRE1 Dependent Decay (RIDD)
ISSN:0024-3205, 1879-0631, 1879-0631
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Shrnutí:The endoplasmic reticulum is primarily responsible for protein folding and maturation. However, the organelle is subject to varied stress conditions from time to time, which lead to the activation of a signaling program known as the Unfolded Protein Response (UPR) pathway. This pathway, upon sensing any disturbance in the protein-folding milieu sends signals to the nucleus and cytoplasm in order to restore homeostasis. One of the prime UPR signaling sensors is Inositol-requiring enzyme 1 (IRE1); an ER membrane embedded protein with dual enzyme activities, kinase and endoribonuclease. The ribonuclease activity of IRE1 results in Xbp1 splicing in mammals or Hac1 splicing in yeast. However, IRE1 can switch its substrate specificity to the mRNAs that are co-transnationally transported to the ER, a phenomenon known as Regulated IRE1 Dependent Decay (RIDD). IRE1 is also reported to act as a principal molecule that coordinates with other proteins and signaling pathways, which in turn might be responsible for its regulation. The current review highlights studies on IRE1 explaining the structural features and molecular mechanism behind its ribonuclease outputs. The emphasis is also laid on the molecular effectors, which directly or indirectly interact with IRE1 to either modulate its function or connect it to other pathways. This is important in understanding the functional pleiotropy of IRE1, by which it can switch its activity from pro-survival to pro-apoptotic, thus determining the fate of cells. [Display omitted]
Bibliografia:ObjectType-Article-1
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ISSN:0024-3205
1879-0631
1879-0631
DOI:10.1016/j.lfs.2020.118740