The unfolded protein response: No longer just a special teams player

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Volumn 2, Issue 8, 2001, Pages 515-523

  Spear, E ^a   Ng, D T W ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

Endoplasmic reticulum; ER associated protein degradation; Gene regulation; Secretory pathway; Signal transduction; Unfolded protein response

Indexed keywords

CHAPERONE;

ANIMAL CELL; BIOCHEMISTRY; CELL FUNCTION; CELL NUCLEUS; CONTROLLED STUDY; CYTOLOGY; DEVELOPMENT; ENDOPLASMIC RETICULUM; GENE; GENETICS; MAMMAL; MOLECULAR BIOLOGY; MONITORING; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; REGULATORY MECHANISM; REVIEW; SIGNAL TRANSDUCTION; STRESS; YEAST;

ANIMALS; CELL NUCLEUS; ENDOPLASMIC RETICULUM; FUNGAL PROTEINS; HUMANS; MODELS, BIOLOGICAL; PROTEIN DENATURATION; PROTEIN FOLDING; SIGNAL TRANSDUCTION; STRESS;

EID: 0034904040     PISSN: 13989219     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-0854.2001.20801.x     Document Type: Review

References (66)

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3. A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins
4. The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum
5. Palindrome with spacer of one nucleotide is characteristic of the cis-acting unfolded protein response element in Saccharomyces cerevisiae
6. Transcriptional induction of genes encoding ER resident proteins requires a transmembrane protein kinase
7. A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus
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13. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
14. The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern 1p) are required for kinase activation
15. Protein serine/threonine phosphatase Ptc2p negatively regulates the unfolded-protein response by dephosphorylating Ire1p kinase
16. A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
17. Endoplasmic reticulum stress-induced mRNA splicing permits synthesis of transcription factor Hac1p/Ern4p that activates the unfolded protein response
18. The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response
19. tRNA ligase is required for regulated mRNA splicing in the unfolded protein response
20. Translational attenuation mediated by an mRNA intron
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22. Gene induction in response to unfolded protein in the endoplasmic reticulum is mediated through Ire1p kinase interaction with a transcriptional coactivator complex containing Ada5p
23. The transcriptional co-activator ADA5 is required for HAC1 mRNA processing in vivo
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25. Cloning of mammalian Ire1 reveals diversity in the ER stress responses
26. Translational control by the ER transmembrane kinase/ribonuclease IRE1 under ER stress
27. Increased sensitivity to dextran sodium sulfate colitis in IRE1beta-deficient mice
28. A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response
29. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
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31. Inhibition of translational initiation eukaryotic cells by calcium ionophore
32. Inhibition of protein synthesis and early protein processing by thapsigargin in cultured cells
33. Perk is essential for translational regulation and cell survival during the unfolded protein response
34. Identification of the cisacting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors
35. The mammalian endoplasmic reticulum stress response element consists of an evolutionarily conserved tripartite structure and interacts with a novel stress-inducible complex
36. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
37. Identification of the G13 (cAMP-response-element-binding protein-related protein) gene product related to activating transcription factor 6 as a transcriptional activator of the mammalian unfolded protein response
38. Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
39. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
40. Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response
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42. The unfolded protein response represses nitrogen-starvation induced developmental differentiation in yeast
43. The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control
44. A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
45. CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum
46. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
47. Quality control in the secretory pathway
48. ER protein quality control and proteasome-mediated degradation
49. Endoplasmic reticulum degradation reverse protein flow of no return
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51. A regulatory link between ER-associated protein degradation and the unfolded-protein response
52. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
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54. RAL. Flux of the paramyxovirus hemagglutinin-neuraminidase glycoprotein through the endoplasmic reticulum activates transcription of the GRP78-BiP gene
55. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
56. A pathway for targeting soluble misfolded proteins to the yeast vacuole
57. Different degradation pathways for heterologous glycoproteins in yeast
58. Signals from the stressed endoplasmic reticulum induce C/EBP-homologous protein (CHOP/GADD153)
59. A pathway distinct from the mammalian unfolded protein response regulates expression of endoplasmic reticulum chaperones in non-stressed cells
60. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
61. Conformational changes and disease - Serpins, prions and Alzheimer's
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63. Conformational disease
64. Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response
65. Upregulation of BiP and CHOP by the unfolded-protein response is independent of presenilin expression
66. EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome