ER Ca2+ overload activates the IRE1α signaling and promotes cell survival

[1]  Tao Li,et al.  VMP1 affects endoplasmic reticulum stress sensitivity via differential modulation of the three unfolded protein response arms. , 2023, Cell reports.

[2]  H. Chen,et al.  Protective Role of Hepassocin against Hepatic Endoplasmic Reticulum Stress in Mice , 2022, International journal of molecular sciences.

[3]  Hongmei Liu,et al.  Ca2+ homeostasis maintained by TMCO1 underlies corpus callosum development via ERK signaling , 2022, Cell Death & Disease.

[4]  B. Morales,et al.  The unfolded protein response transcription factor XBP1s ameliorates Alzheimer’s disease by improving synaptic function and proteostasis , 2022, bioRxiv.

[5]  J. Fielitz,et al.  Hidden Agenda - The Involvement of Endoplasmic Reticulum Stress and Unfolded Protein Response in Inflammation-Induced Muscle Wasting , 2022, Frontiers in Immunology.

[6]  N. Seidah,et al.  Caffeine blocks SREBP2-induced hepatic PCSK9 expression to enhance LDLR-mediated cholesterol clearance , 2022, Nature communications.

[7]  T. Tang,et al.  iASPP suppresses Gp78-mediated TMCO1 degradation to maintain Ca2+ homeostasis and control tumor growth and drug resistance , 2022, Proceedings of the National Academy of Sciences.

[8]  E. Powers,et al.  Pharmacologic IRE1/XBP1s activation promotes systemic adaptive remodeling in obesity , 2022, Nature Communications.

[9]  S. Hubchak,et al.  Hepatic X‐Box Binding Protein 1 and Unfolded Protein Response Is Impaired in Weanling Mice With Resultant Hepatic Injury , 2021, Hepatology.

[10]  Cheng Hu,et al.  FOXA3 induction under endoplasmic reticulum stress contributes to non-alcoholic fatty liver disease. , 2021, Journal of hepatology.

[11]  R. Austin,et al.  Calcium as a reliable marker for the quantitative assessment of endoplasmic reticulum stress in live cells , 2021, The Journal of biological chemistry.

[12]  A. Regev,et al.  QRICH1 dictates the outcome of ER stress through transcriptional control of proteostasis , 2021, Science.

[13]  E. Powers,et al.  Pharmacologic IRE1/XBP1s activation promotes systemic adaptive remodeling in obesity , 2020, Nature Communications.

[14]  D. Ron,et al.  Calcium depletion challenges endoplasmic reticulum proteostasis by destabilising BiP-substrate complexes , 2020, bioRxiv.

[15]  R. L. Wiseman,et al.  Small molecule strategies to harness the unfolded protein response: where do we go from here? , 2020, The Journal of Biological Chemistry.

[16]  B. Ehrlich,et al.  Wolfram Syndrome: a Monogenic Model to Study Diabetes Mellitus and Neurodegeneration. , 2020, Current opinion in physiology.

[17]  Shao-Cong Sun,et al.  A Molecular Mechanism for Turning Off IRE1α Signaling during Endoplasmic Reticulum Stress , 2020, bioRxiv.

[18]  Ningjia He,et al.  Visible light excited ratiometric-GECIs for long-term in-cellulo monitoring of calcium signals. , 2020, Cell calcium.

[19]  M. Mayer,et al.  Unstructured regions in IRE1α specify BiP-mediated destabilisation of the luminal domain dimer and repression of the UPR , 2019, eLife.

[20]  Shijiao Huang,et al.  Emerging roles for the ER stress sensor IRE1α in metabolic regulation and disease , 2019, The Journal of Biological Chemistry.

[21]  Hyunmi Kim,et al.  Parkinson’s disease-associated LRRK2-G2019S mutant acts through regulation of SERCA activity to control ER stress in astrocytes , 2019, Acta Neuropathologica Communications.

[22]  J. Qin,et al.  TMCO1-mediated Ca2+ leak underlies osteoblast functions via CaMKII signaling , 2019, Nature Communications.

[23]  P. Walter,et al.  The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic Reticulum. , 2019, Cold Spring Harbor perspectives in biology.

[24]  Seunghyung Lee,et al.  Tunicamycin-Induced ER Stress is Accompanied with Oxidative Stress via Abrogation of Sulfur Amino Acids Metabolism in the Liver , 2018, International journal of molecular sciences.

[25]  L. Terada,et al.  ROS signaling and ER stress in cardiovascular disease. , 2018, Molecular aspects of medicine.

[26]  S. Battaglia-Hsu,et al.  Endoplasmic Reticulum Stress in Metabolic Disorders , 2018, Cells.

[27]  Jiu-qiang Wang,et al.  TMCO1 is essential for ovarian follicle development by regulating ER Ca2+ store of granulosa cells , 2018, Cell Death & Differentiation.

[28]  M. Vasseur-Cognet,et al.  Interactome Screening Identifies the ER Luminal Chaperone Hsp47 as a Regulator of the Unfolded Protein Response Transducer IRE1α. , 2018, Molecular cell.

[29]  Maruf M. U. Ali,et al.  In vitro FRET analysis of IRE1 and BiP association and dissociation upon endoplasmic reticulum stress , 2018, eLife.

[30]  D. Ron,et al.  A J-Protein Co-chaperone Recruits BiP to Monomerize IRE1 and Repress the Unfolded Protein Response , 2017, Cell.

[31]  S. Christensen,et al.  Inhibition of the sarco/endoplasmic reticulum (ER) Ca2+-ATPase by thapsigargin analogs induces cell death via ER Ca2+ depletion and the unfolded protein response , 2017, The Journal of Biological Chemistry.

[32]  R. Kaufman,et al.  Physiological/pathological ramifications of transcription factors in the unfolded protein response , 2017, Genes & development.

[33]  D. James Surmeier,et al.  Selective neuronal vulnerability in Parkinson disease , 2017, Nature Reviews Neuroscience.

[34]  A. Prat,et al.  Endoplasmic Reticulum Stress and Ca2+ Depletion Differentially Modulate the Sterol Regulatory Protein PCSK9 to Control Lipid Metabolism* , 2016, The Journal of Biological Chemistry.

[35]  U. Wüllner,et al.  The Machado–Joseph Disease Deubiquitinase Ataxin-3 Regulates the Stability and Apoptotic Function of p53 , 2016, PLoS biology.

[36]  M. Iino,et al.  Genetically Encoded Fluorescent Indicators for Organellar Calcium Imaging. , 2016, Biophysical journal.

[37]  S. Sengupta,et al.  Oxidative Homeostasis Regulates the Response to Reductive Endoplasmic Reticulum Stress through Translation Control. , 2016, Cell reports.

[38]  Qinglian Liu,et al.  Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP. , 2015, Structure.

[39]  S. Kersten,et al.  IRE1α is an endogenous substrate of endoplasmic reticulum-associated degradation , 2015, Nature Cell Biology.

[40]  L. Hendershot,et al.  Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linker , 2015, eLife.

[41]  M. Michalak,et al.  Ca(2+) homeostasis and endoplasmic reticulum (ER) stress: An integrated view of calcium signaling. , 2015, Biochemical and biophysical research communications.

[42]  G. Morgan,et al.  Cleavage of BLOC1S1 mRNA by IRE1 Is Sequence Specific, Temporally Separate from XBP1 Splicing, and Dispensable for Cell Viability under Acute Endoplasmic Reticulum Stress , 2015, Molecular and Cellular Biology.

[43]  W. Jia,et al.  Role for the endoplasmic reticulum stress sensor IRE1α in liver regenerative responses. , 2015, Journal of hepatology.

[44]  Maruf M. U. Ali,et al.  Noncanonical binding of BiP ATPase domain to Ire1 and Perk is dissociated by unfolded protein CH1 to initiate ER stress signaling , 2015, eLife.

[45]  Yan-song Wang,et al.  Actinomycin D inhibits cell proliferations and promotes apoptosis in osteosarcoma cells. , 2015, International journal of clinical and experimental medicine.

[46]  J. Tavernier,et al.  Getting RIDD of RNA: IRE1 in cell fate regulation. , 2014, Trends in biochemical sciences.

[47]  F. Brandizzi,et al.  IRE1: ER stress sensor and cell fate executor. , 2013, Trends in cell biology.

[48]  H. Perlman,et al.  Toll‐like receptor‐mediated IRE1α activation as a therapeutic target for inflammatory arthritis , 2013, The EMBO journal.

[49]  Lisa M. Ryno,et al.  Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments. , 2013, Cell reports.

[50]  J. Lechleiter,et al.  Luminal Ca2+ depletion during the unfolded protein response in Xenopus oocytes: cause and consequence. , 2013, Cell calcium.

[51]  D. Ron,et al.  Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains , 2013, Proceedings of the National Academy of Sciences.

[52]  Michael T. McManus,et al.  IRE1α Cleaves Select microRNAs During ER Stress to Derepress Translation of Proapoptotic Caspase-2 , 2012, Science.

[53]  P. Walter,et al.  The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation , 2011, Science.

[54]  D. Mekahli,et al.  Endoplasmic-reticulum calcium depletion and disease. , 2011, Cold Spring Harbor perspectives in biology.

[55]  C. Hetz,et al.  Modulating stress responses by the UPRosome: a matter of life and death. , 2011, Trends in biochemical sciences.

[56]  P. Walter,et al.  Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering , 2010, Proceedings of the National Academy of Sciences.

[57]  Gökhan S Hotamisligil,et al.  Endoplasmic reticulum stress and atherosclerosis , 2010, Nature Medicine.

[58]  E. Puffenberger,et al.  Homozygous frameshift mutation in TMCO1 causes a syndrome with craniofacial dysmorphism, skeletal anomalies, and mental retardation , 2009, Proceedings of the National Academy of Sciences.

[59]  C. Hetz,et al.  Fine-tuning of the unfolded protein response: Assembling the IRE1alpha interactome. , 2009, Molecular cell.

[60]  F. R. Papa,et al.  IRE1α Kinase Activation Modes Control Alternate Endoribonuclease Outputs to Determine Divergent Cell Fates , 2009, Cell.

[61]  D. Surmeier,et al.  Calcium homeostasis, selective vulnerability and Parkinson's disease , 2009, Trends in Neurosciences.

[62]  I. Bezprozvanny.  Calcium signaling and neurodegenerative diseases. , 2009, Trends in molecular medicine.

[63]  Chao Zhang,et al.  The unfolded protein response signals through high-order assembly of Ire1 , 2009, Nature.

[64]  Ilya Bezprozvanny,et al.  Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease , 2008, Trends in Neurosciences.

[65]  D. Stolz,et al.  Differential Effects of Endoplasmic Reticulum Stress-induced Autophagy on Cell Survival* , 2007, Journal of Biological Chemistry.

[66]  Jonathan S Weissman,et al.  Decay of Endoplasmic Reticulum-Localized mRNAs During the Unfolded Protein Response , 2006, Science.

[67]  S. Korsmeyer,et al.  Proapoptotic BAX and BAK Modulate the Unfolded Protein Response by a Direct Interaction with IRE1α , 2006, Science.

[68]  I. Charles,et al.  The Affinity of a Major Ca2+ Binding Site on GRP78 Is Differentially Enhanced by ADP and ATP* , 2006, Journal of Biological Chemistry.

[69]  David B. Williams.  Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum , 2006, Journal of Cell Science.

[70]  J. Szeberényi.  The effect of actinomycin D on RNA metabolism in human cells , 2006, Biochemistry and Molecular Biology Education.

[71]  John Calvin Reed,et al.  Endoplasmic reticulum stress: cell life and death decisions. , 2005, The Journal of clinical investigation.

[72]  D. Ron,et al.  CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. , 2004, Genes & development.

[73]  L. Hendershot,et al.  ER chaperone functions during normal and stress conditions , 2004, Journal of Chemical Neuroanatomy.

[74]  L. Glimcher,et al.  XBP-1 Regulates a Subset of Endoplasmic Reticulum Resident Chaperone Genes in the Unfolded Protein Response , 2003, Molecular and Cellular Biology.

[75]  S. Hotop,et al.  Loading neurons with BAPTA-AM activates xbp1 processing indicative of induction of endoplasmic reticulum stress. , 2003, Cell calcium.

[76]  M Opas,et al.  Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum. , 2002, Cell calcium.

[77]  Lauren Mackenzie,et al.  2‐Aminoethoxydiphenyl borate (2‐APB) is a reliable blocker of store‐operated Ca2+ entry but an inconsistent inhibitor of InsP3‐induced Ca2+ release , 2002, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[78]  Xi Chen,et al.  ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. , 2002, Developmental cell.

[79]  R. Wek,et al.  Dimerization and Release of Molecular Chaperone Inhibition Facilitate Activation of Eukaryotic Initiation Factor-2 Kinase in Response to Endoplasmic Reticulum Stress* , 2002, The Journal of Biological Chemistry.

[80]  K. Mori,et al.  XBP1 mRNA Is Induced by ATF6 and Spliced by IRE1 in Response to ER Stress to Produce a Highly Active Transcription Factor , 2001, Cell.

[81]  R. Kaufman,et al.  Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response. , 2000, The Journal of biological chemistry.

[82]  R. Kaufman,et al.  Ligand-independent Dimerization Activates the Stress Response Kinases IRE1 and PERK in the Lumen of the Endoplasmic Reticulum* , 2000, The Journal of Biological Chemistry.

[83]  Anne Bertolotti,et al.  Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response , 2000, Nature Cell Biology.

[84]  Peter Walter,et al.  Functional and Genomic Analyses Reveal an Essential Coordination between the Unfolded Protein Response and ER-Associated Degradation , 2000, Cell.

[85]  F. Urano,et al.  Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. , 2000, Science.

[86]  Masahiko Kuroda,et al.  Cloning of mammalian Ire1 reveals diversity in the ER stress responses , 1998, The EMBO journal.

[87]  J. Meldolesi,et al.  BiP, a Major Chaperone Protein of the Endoplasmic Reticulum Lumen, Plays a Direct and Important Role in the Storage of the Rapidly Exchanging Pool of Ca2+ * , 1997, The Journal of Biological Chemistry.

[88]  L. Hendershot,et al.  The modification and assembly of proteins in the endoplasmic reticulum. , 1993, Current opinion in cell biology.

[89]  Peter Walter,et al.  Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase , 1993, Cell.

[90]  S. Baksh,et al.  Expression of calreticulin in Escherichia coli and identification of its Ca2+ binding domains. , 1991, The Journal of biological chemistry.

[91]  J. Rothman,et al.  Peptide-binding specificity of the molecular chaperone BiP , 1991, Nature.

[92]  P. H. Cameron,et al.  SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. , 1991, The Journal of biological chemistry.

[93]  H. Söling,et al.  Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium. No indication for calsequestrin-like proteins in inositol 1,4,5-trisphosphate-sensitive calcium sequestering rat liver vesicles. , 1989, The Journal of biological chemistry.

[94]  D. Macer,et al.  Identification of a set of calcium-binding proteins in reticuloplasm, the luminal content of the endoplasmic reticulum. , 1988, Journal of cell science.

[95]  M. Michalak,et al.  Calcium binding chaperones of the endoplasmic reticulum. , 2009, General physiology and biophysics.

[96]  D. Wildman,et al.  Proapoptotic BAX and BAK Modulate the Unfolded Protein Response by a Direct Interaction with IRE1a , 2006 .

[97]  Hilde van der Togt,et al.  Publisher's Note , 2003, J. Netw. Comput. Appl..

[98]  Dustin J Maly,et al.  Title Targeting ABL-IRE 1 alpha Signaling Spares ER-Stressed Pancreatic beta Cells to Reverse Autoimmune Diabetes , 2022 .