Signal integration in the endoplasmic reticulum unfolded protein response (Q27860577)

Nature Reviews Molecular Cell Biology

Europe PubMed Central

title

Signal integration in the endoplasmic reticulum unfolded protein response (English)

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main subject

endoplasmic reticulum

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author

David Ron

series ordinal

1

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author name string

Peter Walter

series ordinal

2

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language of work or name

English

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publication date

July 2007

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published in

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volume

8

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issue

7

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page(s)

519-29

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cites work

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The mammalian unfolded protein response

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Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase

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A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus

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On the mechanism of sensing unfolded protein in the endoplasmic reticulum

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The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response

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Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus

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Bypassing a Kinase Activity with an ATP-Competitive Drug

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A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response

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Signalling from endoplasmic reticulum to nucleus: transcription factor with a basic-leucine zipper motif is required for the unfolded protein-response pathway

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XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor

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IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA

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tRNA ligase is required for regulated mRNA splicing in the unfolded protein response

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Stable ribosome binding to the endoplasmic reticulum enables compartment-specific regulation of mRNA translation

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Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response

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pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response

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IRE1-independent gain control of the unfolded protein response

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Functionality of unspliced XBP1 is required to explain evolution of overlapping reading frames

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Genetic interactions due to constitutive and inducible gene regulation mediated by the unfolded protein response in C. elegans.

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Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1

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Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress

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Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha

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ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats

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Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response.

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Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress

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ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs

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ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals

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Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response

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Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response

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Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

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An integrated stress response regulates amino acid metabolism and resistance to oxidative stress

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Translational control is required for the unfolded protein response and in vivo glucose homeostasis

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Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2

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Gcn4p, a master regulator of gene expression, is controlled at multiple levels by diverse signals of starvation and stress

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Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells

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Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response

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Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 is required for activation of NF-kappaB in response to diverse cellular stresses

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Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2

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Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells

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Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1.

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Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha

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Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress

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Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2

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Stress-induced gene expression requires programmed recovery from translational repression

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Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival

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A time-dependent phase shift in the mammalian unfolded protein response

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Gcn4p and novel upstream activating sequences regulate targets of the unfolded protein response

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Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation

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Diverse and specific gene expression responses to stresses in cultured human cells

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Regulated translation initiation controls stress-induced gene expression in mammalian cells

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BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum

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Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway

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The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane

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Plasma cell differentiation requires the transcription factor XBP-1

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XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands

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XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation

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XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum.

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Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response

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Enrichment of endoplasmic reticulum with cholesterol inhibits sarcoplasmic-endoplasmic reticulum calcium ATPase-2b activity in parallel with increased order of membrane lipids: implications for depletion of endoplasmic reticulum calcium stores and a

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The endoplasmic reticulum is the site of cholesterol-induced cytotoxicity in macrophages

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Bioactive small molecules reveal antagonism between the integrated stress response and sterol-regulated gene expression

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ATF6 modulates SREBP2-mediated lipogenesis.

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Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes

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Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes

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Endoplasmic reticulum stress triggers autophagy

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Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis

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Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death

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Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta

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Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins

31 March 2020

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Perk is essential for translational regulation and cell survival during the unfolded protein response

31 March 2020

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Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state

31 March 2020

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CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum

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Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes

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CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum

31 March 2020

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A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress

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Regulation of antioxidant metabolism by translation initiation factor 2alpha

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CHOP/GADD153 is a mediator of apoptotic death in substantia nigra dopamine neurons in an in vivo neurotoxin model of parkinsonism

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The role of the unfolded protein response in tumour development: friend or foe?

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Hsp90 as a capacitor of phenotypic variation

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Gene expression during acute and prolonged hypoxia is regulated by distinct mechanisms of translational control

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Activating transcription factor 4 is translationally regulated by hypoxic stress

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ER stress-regulated translation increases tolerance to extreme hypoxia and promotes tumor growth

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The unfolded protein response: a novel component of the hypoxic stress response in tumors.

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Inhibition of tumor progression by suppression of stress protein GRP78/BiP induction in fibrosarcoma B/C10ME.

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Perk-dependent translational regulation promotes tumor cell adaptation and angiogenesis in response to hypoxic stress

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XBP1 is essential for survival under hypoxic conditions and is required for tumor growth.

31 March 2020

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The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response

31 March 2020

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Activation-dependent substrate recruitment by the eukaryotic translation initiation factor 2 kinase PERK.

31 March 2020

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Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis

31 March 2020

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BAX and BAK regulation of endoplasmic reticulum Ca2+: a control point for apoptosis

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NRM2199

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Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

37458

1020759434

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37458

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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