Phosphorylation of IRE1 at S729 regulates RIDD in B cells and antibody production after immunization

To relieve endoplasmic reticulum (ER) stress, IRE1 splices XBP1 messenger RNA (mRNA) or engages regulated IRE1-dependent decay (RIDD) of other mRNAs. Upon XBP1 deficiency, IRE1 switches to perform RIDD. We examined IRE1 in XBP1-deficient B cells and discovered that IRE1 undergoes phosphorylation at...

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Published in	The Journal of cell biology Vol. 217; no. 5; pp. 1739 - 1755
Main Authors	Tang, Chih-Hang Anthony, Chang, Shiun, Paton, Adrienne W., Paton, James C., Gabrilovich, Dmitry I., Ploegh, Hidde L., Del Valle, Juan R., Hu, Chih-Chi Andrew
Format	Journal Article
Language	English
Published	United States Rockefeller University Press 07.05.2018
Subjects	Amino Acid Sequence Animals Antibody Formation B-Lymphocytes - metabolism Dithiothreitol - pharmacology Endoplasmic reticulum Endoplasmic Reticulum Stress - drug effects Immunization Immunoglobulin G - blood Immunoglobulin M - blood Immunoglobulins Lipopolysaccharides Lymphocytes B Membrane Proteins - chemistry Membrane Proteins - metabolism Mice Mice, Inbred C57BL Models, Animal Models, Biological mRNA Pharmacology Phosphorylation Phosphoserine - metabolism Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - metabolism Ribonucleic acid RNA RNA Stability Stresses Subtilase Switches T-Lymphocytes - metabolism Toll-like receptors Up-Regulation - drug effects X-Box Binding Protein 1 - metabolism
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ISSN	0021-9525 1540-8140 1540-8140
DOI	10.1083/jcb.201709137

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Abstract	To relieve endoplasmic reticulum (ER) stress, IRE1 splices XBP1 messenger RNA (mRNA) or engages regulated IRE1-dependent decay (RIDD) of other mRNAs. Upon XBP1 deficiency, IRE1 switches to perform RIDD. We examined IRE1 in XBP1-deficient B cells and discovered that IRE1 undergoes phosphorylation at S729. We generated an anti–phospho-S729 antibody to investigate such phosphorylation. Compared with pharmacological ER stress inducers or Toll-like receptor ligands, the bacterial subtilase cytotoxin has an unusual capability in causing rapid and strong phosphorylation at S729 and triggering B cells to express spliced XBP1. To assess the function of S729 in IRE1, we generated S729A knock-in mice and found S729 is critically important for lipopolysaccharide-stimulated plasmablasts to respond to additional ER stress and for antibody production in response to immunization. We further crossed mice carrying an S729A mutation or ΔIRE1 (missing the kinase domain) with B cell–specific XBP1-deficient mice to trigger RIDD and discovered a critical role for S729 in regulating RIDD in B cells.
AbstractList	To relieve endoplasmic reticulum (ER) stress, IRE1 splices XBP1 messenger RNA (mRNA) or engages regulated IRE1-dependent decay (RIDD) of other mRNAs. Upon XBP1 deficiency, IRE1 switches to perform RIDD. We examined IRE1 in XBP1-deficient B cells and discovered that IRE1 undergoes phosphorylation at S729. We generated an anti-phospho-S729 antibody to investigate such phosphorylation. Compared with pharmacological ER stress inducers or Toll-like receptor ligands, the bacterial subtilase cytotoxin has an unusual capability in causing rapid and strong phosphorylation at S729 and triggering B cells to express spliced XBP1. To assess the function of S729 in IRE1, we generated S729A knock-in mice and found S729 is critically important for lipopolysaccharide-stimulated plasmablasts to respond to additional ER stress and for antibody production in response to immunization. We further crossed mice carrying an S729A mutation or ΔIRE1 (missing the kinase domain) with B cell-specific XBP1-deficient mice to trigger RIDD and discovered a critical role for S729 in regulating RIDD in B cells. Phosphorylation of IRE1 at S729 enhances splicing of XBP1 messenger RNA and regulates RIDD. lipopolysaccharide-stimulated plasmablasts from S729A knock-in mice fail to boost spliced XBP1 in response to ER stress. Such mice exhibit plasma cells with decreased numbers and altered functions after immunization. To relieve endoplasmic reticulum (ER) stress, IRE1 splices XBP1 messenger RNA (mRNA) or engages regulated IRE1-dependent decay (RIDD) of other mRNAs. Upon XBP1 deficiency, IRE1 switches to perform RIDD. We examined IRE1 in XBP1-deficient B cells and discovered that IRE1 undergoes phosphorylation at S729. We generated an anti–phospho-S729 antibody to investigate such phosphorylation. Compared with pharmacological ER stress inducers or Toll-like receptor ligands, the bacterial subtilase cytotoxin has an unusual capability in causing rapid and strong phosphorylation at S729 and triggering B cells to express spliced XBP1. To assess the function of S729 in IRE1, we generated S729A knock-in mice and found S729 is critically important for lipopolysaccharide-stimulated plasmablasts to respond to additional ER stress and for antibody production in response to immunization. We further crossed mice carrying an S729A mutation or ΔIRE1 (missing the kinase domain) with B cell–specific XBP1-deficient mice to trigger RIDD and discovered a critical role for S729 in regulating RIDD in B cells. To relieve endoplasmic reticulum (ER) stress, IRE1 splices XBP1 messenger RNA (mRNA) or engages regulated IRE1-dependent decay (RIDD) of other mRNAs. Upon XBP1 deficiency, IRE1 switches to perform RIDD. We examined IRE1 in XBP1-deficient B cells and discovered that IRE1 undergoes phosphorylation at S729. We generated an anti-phospho-S729 antibody to investigate such phosphorylation. Compared with pharmacological ER stress inducers or Toll-like receptor ligands, the bacterial subtilase cytotoxin has an unusual capability in causing rapid and strong phosphorylation at S729 and triggering B cells to express spliced XBP1. To assess the function of S729 in IRE1, we generated S729A knock-in mice and found S729 is critically important for lipopolysaccharide-stimulated plasmablasts to respond to additional ER stress and for antibody production in response to immunization. We further crossed mice carrying an S729A mutation or ΔIRE1 (missing the kinase domain) with B cell-specific XBP1-deficient mice to trigger RIDD and discovered a critical role for S729 in regulating RIDD in B cells.To relieve endoplasmic reticulum (ER) stress, IRE1 splices XBP1 messenger RNA (mRNA) or engages regulated IRE1-dependent decay (RIDD) of other mRNAs. Upon XBP1 deficiency, IRE1 switches to perform RIDD. We examined IRE1 in XBP1-deficient B cells and discovered that IRE1 undergoes phosphorylation at S729. We generated an anti-phospho-S729 antibody to investigate such phosphorylation. Compared with pharmacological ER stress inducers or Toll-like receptor ligands, the bacterial subtilase cytotoxin has an unusual capability in causing rapid and strong phosphorylation at S729 and triggering B cells to express spliced XBP1. To assess the function of S729 in IRE1, we generated S729A knock-in mice and found S729 is critically important for lipopolysaccharide-stimulated plasmablasts to respond to additional ER stress and for antibody production in response to immunization. We further crossed mice carrying an S729A mutation or ΔIRE1 (missing the kinase domain) with B cell-specific XBP1-deficient mice to trigger RIDD and discovered a critical role for S729 in regulating RIDD in B cells.
Author	Tang, Chih-Hang Anthony Paton, Adrienne W. Gabrilovich, Dmitry I. Del Valle, Juan R. Paton, James C. Hu, Chih-Chi Andrew Ploegh, Hidde L. Chang, Shiun
AuthorAffiliation	2 Department of Molecular and Cellular Biology, Research Centre for Infectious Diseases, University of Adelaide, Adelaide, Australia 4 Department of Chemistry, University of South Florida, Tampa, FL 1 The Wistar Institute, Philadelphia, PA 3 Program in Cellular and Molecular Medicine, Boston Children’s Hospital, Boston, MA
AuthorAffiliation_xml	– name: 1 The Wistar Institute, Philadelphia, PA – name: 2 Department of Molecular and Cellular Biology, Research Centre for Infectious Diseases, University of Adelaide, Adelaide, Australia – name: 3 Program in Cellular and Molecular Medicine, Boston Children’s Hospital, Boston, MA – name: 4 Department of Chemistry, University of South Florida, Tampa, FL
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Snippet	To relieve endoplasmic reticulum (ER) stress, IRE1 splices XBP1 messenger RNA (mRNA) or engages regulated IRE1-dependent decay (RIDD) of other mRNAs. Upon XBP1... Phosphorylation of IRE1 at S729 enhances splicing of XBP1 messenger RNA and regulates RIDD. lipopolysaccharide-stimulated plasmablasts from S729A knock-in mice...
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SubjectTerms	Amino Acid Sequence Animals Antibody Formation B-Lymphocytes - metabolism Dithiothreitol - pharmacology Endoplasmic reticulum Endoplasmic Reticulum Stress - drug effects Immunization Immunoglobulin G - blood Immunoglobulin M - blood Immunoglobulins Lipopolysaccharides Lymphocytes B Membrane Proteins - chemistry Membrane Proteins - metabolism Mice Mice, Inbred C57BL Models, Animal Models, Biological mRNA Pharmacology Phosphorylation Phosphoserine - metabolism Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - metabolism Ribonucleic acid RNA RNA Stability Stresses Subtilase Switches T-Lymphocytes - metabolism Toll-like receptors Up-Regulation - drug effects X-Box Binding Protein 1 - metabolism
Title	Phosphorylation of IRE1 at S729 regulates RIDD in B cells and antibody production after immunization
URI	https://www.ncbi.nlm.nih.gov/pubmed/29511123 https://www.proquest.com/docview/2078823263 https://www.proquest.com/docview/2011614731 https://pubmed.ncbi.nlm.nih.gov/PMC5940306
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