Structure and Molecular Mechanism of ER Stress Signaling by the Unfolded Protein Response Signal Activator IRE1

The endoplasmic reticulum (ER) is an important site for protein folding and maturation in eukaryotes. The cellular requirement to synthesize proteins within the ER is matched by its folding capacity. However, the physiological demands or aberrations in folding may result in an imbalance which can le...

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Vydáno v:Frontiers in molecular biosciences Ročník 6; s. 11
Hlavní autoři: Adams, Christopher J., Kopp, Megan C., Larburu, Natacha, Nowak, Piotr R., Ali, Maruf M. U.
Médium: Journal Article
Jazyk:angličtina
Vydáno: Switzerland Frontiers Media S.A 12.03.2019
Témata:
BiP
crystal structures
ER stress
Hsp70
IRE1 inositol-requiring enzyme 1
Molecular Biosciences
unfolded protein response (UPR)
BiP
ER stress
Hsp70
IRE1 inositol-requiring enzyme 1
crystal structures
unfolded protein response (UPR)
ISSN:2296-889X, 2296-889X
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Shrnutí:The endoplasmic reticulum (ER) is an important site for protein folding and maturation in eukaryotes. The cellular requirement to synthesize proteins within the ER is matched by its folding capacity. However, the physiological demands or aberrations in folding may result in an imbalance which can lead to the accumulation of misfolded protein, also known as "ER stress." The unfolded protein response (UPR) is a cell-signaling system that readjusts ER folding capacity to restore protein homeostasis. The key UPR signal activator, IRE1, responds to stress by propagating the UPR signal from the ER to the cytosol. Here, we discuss the structural and molecular basis of IRE1 stress signaling, with particular focus on novel mechanistic advances. We draw a comparison between the recently proposed allosteric model for UPR induction and the role of Hsp70 during polypeptide import to the mitochondrial matrix.
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Reviewed by: Sebastian Schuck, Universität Heidelberg, Germany; Robert Ernst, Saarland University, Germany
This article was submitted to Protein Folding, Misfolding and Degradation, a section of the journal Frontiers in Molecular Biosciences
Edited by: Matthias Peter Mayer, Universität Heidelberg, Germany
ISSN:2296-889X
2296-889X
DOI:10.3389/fmolb.2019.00011