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  • 1
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    Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1 (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-29
    Description: Malfolded proteins in the endoplasmic reticulum (ER) induce cellular stress and activate c-Jun amino-terminal kinases (JNKs or SAPKs). Mammalian homologs of yeast IRE1, which activate chaperone genes in response to ER stress, also activated JNK, and IRE1alpha-/- fibroblasts were impaired in JNK activation by ER stress. The cytoplasmic part of IRE1 bound TRAF2, an adaptor protein that couples plasma membrane receptors to JNK activation. Dominant-negative TRAF2 inhibited activation of JNK by IRE1. Activation of JNK by endogenous signals initiated in the ER proceeds by a pathway similar to that initiated by cell surface receptors in response to extracellular signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Urano, F -- Wang, X -- Bertolotti, A -- Zhang, Y -- Chung, P -- Harding, H P -- Ron, D -- DK47119/DK/NIDDK NIH HHS/ -- ES08681/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jan 28;287(5453):664-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Skirball Institute of Biomolecular Medicine, Departments of Medicine, Cell Biology and the Kaplan Cancer Center, New York University Medical School, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10650002" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cells, Cultured ; Endoplasmic Reticulum/*metabolism ; Endoribonucleases/genetics/*metabolism ; Enzyme Activation ; Gene Targeting ; Humans ; JNK Mitogen-Activated Protein Kinases ; *Membrane Proteins ; Mitogen-Activated Protein Kinases/*metabolism ; Multienzyme Complexes/genetics/*metabolism ; Protein Kinases/genetics/*metabolism ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Proteins/chemistry/genetics/*metabolism ; Rats ; Recombinant Fusion Proteins/metabolism ; TNF Receptor-Associated Factor 2 ; Thapsigargin/pharmacology ; Two-Hybrid System Techniques ; eIF-2 Kinase/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-12
    Description: Most protein phosphatases have little intrinsic substrate specificity, making selective pharmacological inhibition of specific dephosphorylation reactions a challenging problem. In a screen for small molecules that protect cells from endoplasmic reticulum (ER) stress, we identified salubrinal, a selective inhibitor of cellular complexes that dephosphorylate eukaryotic translation initiation factor 2 subunit alpha (eIF2alpha). Salubrinal also blocks eIF2alpha dephosphorylation mediated by a herpes simplex virus protein and inhibits viral replication. These results suggest that selective chemical inhibitors of eIF2alpha dephosphorylation may be useful in diseases involving ER stress or viral infection. More broadly, salubrinal demonstrates the feasibility of selective pharmacological targeting of cellular dephosphorylation events.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boyce, Michael -- Bryant, Kevin F -- Jousse, Celine -- Long, Kai -- Harding, Heather P -- Scheuner, Donalyn -- Kaufman, Randal J -- Ma, Dawei -- Coen, Donald M -- Ron, David -- Yuan, Junying -- AI19838/AI/NIAID NIH HHS/ -- AI26077/AI/NIAID NIH HHS/ -- DDK42394/DK/NIDDK NIH HHS/ -- DK47119/DK/NIDDK NIH HHS/ -- ES08681/ES/NIEHS NIH HHS/ -- GM64703/GM/NIGMS NIH HHS/ -- NS35138/NS/NINDS NIH HHS/ -- R37-AG012859/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2005 Feb 11;307(5711):935-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15705855" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Differentiation ; Apoptosis/*drug effects ; Cell Cycle Proteins ; Cell Line ; Cinnamates/*pharmacology/toxicity ; *Cytoprotection ; Dose-Response Relationship, Drug ; Endoplasmic Reticulum/*metabolism ; Enzyme Inhibitors/pharmacology ; Eukaryotic Initiation Factor-2/*metabolism ; Genes, Reporter ; Herpesvirus 1, Human/drug effects/physiology ; Keratitis, Herpetic/drug therapy/virology ; Male ; Mice ; Oxazoles/pharmacology/toxicity ; PC12 Cells ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Protein Folding ; Protein Kinases/metabolism ; Protein Phosphatase 1 ; Proteins/metabolism ; Rats ; Thiourea/*analogs & derivatives/*pharmacology/toxicity ; Tunicamycin/pharmacology ; Viral Proteins/metabolism ; Virus Replication/drug effects
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Cell biology. Stressed cells cope with protein overload (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-07-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ron, David -- New York, N.Y. -- Science. 2006 Jul 7;313(5783):52-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Skirball Institute, New York University Medical Center, 540 First Avenue, New York, NY 10016, USA. ron@saturn.med.nyu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16825557" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cytosol/metabolism ; DNA-Binding Proteins/metabolism ; Drosophila Proteins/chemistry/genetics/*metabolism ; Drosophila melanogaster/genetics/metabolism ; Endoplasmic Reticulum/*metabolism ; Endoribonucleases/chemistry/genetics/*metabolism ; Evolution, Molecular ; Gene Expression Regulation ; Membrane Proteins/chemistry/genetics/*metabolism ; Models, Biological ; Protein Biosynthesis ; *Protein Folding ; Protein Sorting Signals/physiology ; Protein Structure, Tertiary ; *RNA Stability ; RNA, Messenger/genetics/*metabolism ; Signal Transduction ; Transcription Factors/metabolism ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Cell biology. A translational pause to localize (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-02-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ron, David -- Ito, Koreaki -- New York, N.Y. -- Science. 2011 Feb 4;331(6017):543-4. doi: 10.1126/science.1202075.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Metabolic Sciences, University of Cambridge, Cambridge, CB2 0QQ, UK. dr360@medschl.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21292960" target="_blank"〉PubMed〈/a〉
    Keywords: DNA-Binding Proteins/chemistry/*genetics/*metabolism ; Endoplasmic Reticulum/*metabolism ; Escherichia coli/genetics/metabolism ; Escherichia coli Proteins/genetics/metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Intracellular Membranes/metabolism ; *Protein Biosynthesis ; Protein Structure, Tertiary ; *RNA Splicing ; RNA, Messenger/*genetics/metabolism ; Ribosomes/metabolism ; Transcription Factors/chemistry/*genetics/*metabolism ; Unfolded Protein Response
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    The unfolded protein response: from stress pathway to homeostatic regulation (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-11-26
    Description: The vast majority of proteins that a cell secretes or displays on its surface first enter the endoplasmic reticulum (ER), where they fold and assemble. Only properly assembled proteins advance from the ER to the cell surface. To ascertain fidelity in protein folding, cells regulate the protein-folding capacity in the ER according to need. The ER responds to the burden of unfolded proteins in its lumen (ER stress) by activating intracellular signal transduction pathways, collectively termed the unfolded protein response (UPR). Together, at least three mechanistically distinct branches of the UPR regulate the expression of numerous genes that maintain homeostasis in the ER or induce apoptosis if ER stress remains unmitigated. Recent advances shed light on mechanistic complexities and on the role of the UPR in numerous diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walter, Peter -- Ron, David -- Howard Hughes Medical Institute/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2011 Nov 25;334(6059):1081-6. doi: 10.1126/science.1209038.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94158, USA. peter@walterlab.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22116877" target="_blank"〉PubMed〈/a〉
    Keywords: Activating Transcription Factor 6/metabolism ; Animals ; Apoptosis ; Endoplasmic Reticulum/*metabolism ; *Endoplasmic Reticulum Stress ; Endoplasmic Reticulum-Associated Degradation ; Endoribonucleases/metabolism ; Gene Expression Regulation ; Homeostasis ; Humans ; Protein-Serine-Threonine Kinases/metabolism ; Proteolysis ; Signal Transduction ; *Unfolded Protein Response ; Yeasts/genetics/metabolism ; eIF-2 Kinase/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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