Trafficking of the bZIP transmembrane transcription factor CREB-H into alternate pathways of ERAD and stress-regulated intramembrane proteolysis. (Q50336411)

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scientific article published on 17 October 2007

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English	Trafficking of the bZIP transmembrane transcription factor CREB-H into alternate pathways of ERAD and stress-regulated intramembrane proteolysis.	scientific article published on 17 October 2007

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

5 March 2018

http://europepmc.org/abstract/MED/17875199

Trafficking of the bZIP transmembrane transcription factor CREB-H into alternate pathways of ERAD and stress-regulated intramembrane proteolysis. (English)

1 reference

Europe PubMed Central

PubMed publication ID

5 March 2018

http://europepmc.org/abstract/MED/17875199

transmembrane protein

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author name string

Daniel Bailey

1

1 reference

Europe PubMed Central

PubMed publication ID

5 March 2018

http://europepmc.org/abstract/MED/17875199

Cristina Barreca

2

1 reference

Europe PubMed Central

PubMed publication ID

5 March 2018

http://europepmc.org/abstract/MED/17875199

Peter O'Hare

3

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Europe PubMed Central

PubMed publication ID

5 March 2018

http://europepmc.org/abstract/MED/17875199

publication date

17 October 2007

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Europe PubMed Central

PubMed publication ID

5 March 2018

http://europepmc.org/abstract/MED/17875199

1 reference

Europe PubMed Central

PubMed publication ID

5 March 2018

http://europepmc.org/abstract/MED/17875199

8

1 reference

Europe PubMed Central

PubMed publication ID

5 March 2018

http://europepmc.org/abstract/MED/17875199

12

1 reference

Europe PubMed Central

PubMed publication ID

5 March 2018

http://europepmc.org/abstract/MED/17875199

1796-1814

1 reference

Europe PubMed Central

PubMed publication ID

5 March 2018

http://europepmc.org/abstract/MED/17875199

ER protein quality control and proteasome-mediated protein degradation

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Folding of newly translated proteins in vivo: the role of molecular chaperones

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Setting the standards: quality control in the secretory pathway

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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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Quality control in the endoplasmic reticulum

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ERAD: the long road to destruction

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Proteolysis and sterol regulation

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Molecular chaperones in the cytosol: from nascent chain to folded protein

1 reference

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Protein quality control: chaperones culling corrupt conformations

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Endoplasmic reticulum-associated degradation

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Checkpoints in ER-associated degradation: excuse me, which way to the proteasome?

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The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor

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SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis

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Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors

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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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Hairpin orientation of sterol regulatory element-binding protein-2 in cell membranes as determined by protease protection

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

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A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

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Cleavage site for sterol-regulated protease localized to a leu-Ser bond in the lumenal loop of sterol regulatory element-binding protein-2.

1 reference

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Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment

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Cleavage of sterol regulatory element-binding proteins (SREBPs) at site-1 requires interaction with SREBP cleavage-activating protein. Evidence from in vivo competition studies

1 reference

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Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs

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Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells

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SREBP-2, a second basic-helix-loop-helix-leucine zipper protein that stimulates transcription by binding to a sterol regulatory element

1 reference

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Regulated cleavage of sterol regulatory element binding proteins requires sequences on both sides of the endoplasmic reticulum membrane

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ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1

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

1 reference

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The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi

1 reference

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Luman, a new member of the CREB/ATF family, binds to herpes simplex virus VP16-associated host cellular factor

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Identification of a novel gene, OASIS, which encodes for a putative CREB/ATF family transcription factor in the long-term cultured astrocytes and gliotic tissue

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Molecular cloning and characterization of a novel human cAMP response element-binding ( CREB) gene ( CREB4).

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Fusion of the FUS and BBF2H7 genes in low grade fibromyxoid sarcoma

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CREB-H: a novel mammalian transcription factor belonging to the CREB/ATF family and functioning via the box-B element with a liver-specific expression

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The liver-enriched transcription factor CREB-H is a growth suppressor protein underexpressed in hepatocellular carcinoma

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

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A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation

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Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins

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Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control

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CREB4, a transmembrane bZip transcription factor and potential new substrate for regulation and cleavage by S1P.

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Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis

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OASIS, a CREB/ATF-family member, modulates UPR signalling in astrocytes

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Transport-Dependent Proteolysis of SREBP

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SREBP pathway responds to sterols and functions as an oxygen sensor in fission yeast

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OASIS is a transcriptional activator of CREB/ATF family with a transmembrane domain

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Identifiers

10.1111/J.1600-0854.2007.00654.X

1 reference

Europe PubMed Central

PubMed publication ID

5 March 2018

http://europepmc.org/abstract/MED/17875199

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 March 2018

http://europepmc.org/abstract/MED/17875199

ResearchGate publication ID

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