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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Autor*in:	Christopher J. Adams [verfasserIn] Megan C. Kopp [verfasserIn] Natacha Larburu [verfasserIn] Piotr R. Nowak [verfasserIn] Maruf M. U. Ali [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2019

Schlagwörter:	unfolded protein response (UPR) IRE1 inositol-requiring enzyme 1 ER stress crystal structures Hsp70 BiP

Übergeordnetes Werk:	In: Frontiers in Molecular Biosciences - Frontiers Media S.A., 2015, 6(2019)
Übergeordnetes Werk:	volume:6 ; year:2019

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3389/fmolb.2019.00011

Katalog-ID:	DOAJ076613178

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520			\|a 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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spelling	10.3389/fmolb.2019.00011 doi (DE-627)DOAJ076613178 (DE-599)DOAJd27d807958cf4c4d93c2aa5d7a0255af DE-627 ger DE-627 rakwb eng QH301-705.5 Christopher J. Adams verfasserin aut Structure and Molecular Mechanism of ER Stress Signaling by the Unfolded Protein Response Signal Activator IRE1 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. unfolded protein response (UPR) IRE1 inositol-requiring enzyme 1 ER stress crystal structures Hsp70 BiP Biology (General) Megan C. Kopp verfasserin aut Natacha Larburu verfasserin aut Piotr R. Nowak verfasserin aut Maruf M. U. Ali verfasserin aut In Frontiers in Molecular Biosciences Frontiers Media S.A., 2015 6(2019) (DE-627)820039691 (DE-600)2814330-9 2296889X nnns volume:6 year:2019 https://doi.org/10.3389/fmolb.2019.00011 kostenfrei https://doaj.org/article/d27d807958cf4c4d93c2aa5d7a0255af kostenfrei https://www.frontiersin.org/article/10.3389/fmolb.2019.00011/full kostenfrei https://doaj.org/toc/2296-889X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2019
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allfieldsSound	10.3389/fmolb.2019.00011 doi (DE-627)DOAJ076613178 (DE-599)DOAJd27d807958cf4c4d93c2aa5d7a0255af DE-627 ger DE-627 rakwb eng QH301-705.5 Christopher J. Adams verfasserin aut Structure and Molecular Mechanism of ER Stress Signaling by the Unfolded Protein Response Signal Activator IRE1 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. unfolded protein response (UPR) IRE1 inositol-requiring enzyme 1 ER stress crystal structures Hsp70 BiP Biology (General) Megan C. Kopp verfasserin aut Natacha Larburu verfasserin aut Piotr R. Nowak verfasserin aut Maruf M. U. Ali verfasserin aut In Frontiers in Molecular Biosciences Frontiers Media S.A., 2015 6(2019) (DE-627)820039691 (DE-600)2814330-9 2296889X nnns volume:6 year:2019 https://doi.org/10.3389/fmolb.2019.00011 kostenfrei https://doaj.org/article/d27d807958cf4c4d93c2aa5d7a0255af kostenfrei https://www.frontiersin.org/article/10.3389/fmolb.2019.00011/full kostenfrei https://doaj.org/toc/2296-889X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2019
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callnumber-first	Q - Science
author	Christopher J. Adams
spellingShingle	Christopher J. Adams misc QH301-705.5 misc unfolded protein response (UPR) misc IRE1 inositol-requiring enzyme 1 misc ER stress misc crystal structures misc Hsp70 misc BiP misc Biology (General) Structure and Molecular Mechanism of ER Stress Signaling by the Unfolded Protein Response Signal Activator IRE1
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topic_title	QH301-705.5 Structure and Molecular Mechanism of ER Stress Signaling by the Unfolded Protein Response Signal Activator IRE1 unfolded protein response (UPR) IRE1 inositol-requiring enzyme 1 ER stress crystal structures Hsp70 BiP
topic	misc QH301-705.5 misc unfolded protein response (UPR) misc IRE1 inositol-requiring enzyme 1 misc ER stress misc crystal structures misc Hsp70 misc BiP misc Biology (General)
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title	Structure and Molecular Mechanism of ER Stress Signaling by the Unfolded Protein Response Signal Activator IRE1
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title_full	Structure and Molecular Mechanism of ER Stress Signaling by the Unfolded Protein Response Signal Activator IRE1
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title_sort	structure and molecular mechanism of er stress signaling by the unfolded protein response signal activator ire1
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title_auth	Structure and Molecular Mechanism of ER Stress Signaling by the Unfolded Protein Response Signal Activator IRE1
abstract	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.
abstractGer	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.
abstract_unstemmed	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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title_short	Structure and Molecular Mechanism of ER Stress Signaling by the Unfolded Protein Response Signal Activator IRE1
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