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    IRE1 bifunctional endoribonuclease/protein kinase IRE1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856478, updated on 9-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Role of Inositol-Requiring Enzyme 1 and Autophagy in the Pro-Fibrotic Mechanism Underlying Graves' Orbitopathy.

    Role of Inositol-Requiring Enzyme 1 and Autophagy in the Pro-Fibrotic Mechanism Underlying Graves' Orbitopathy.
    Lee CE, Kim JY, Yoon JS, Ko J., Free PMC Article

    07/11/2024
    The functional role of Ire1 in regulating autophagy and proteasomal degradation under prolonged proteotoxic stress.

    The functional role of Ire1 in regulating autophagy and proteasomal degradation under prolonged proteotoxic stress.
    Das E, Sahu KK, Roy I.

    06/23/2023
    An ER-accumulated mutant of yeast Pma1 causes membrane-related stress to induce the unfolded protein response.

    An ER-accumulated mutant of yeast Pma1 causes membrane-related stress to induce the unfolded protein response.
    Phuong HT, Ishiwata-Kimata Y, Kimata Y.

    06/15/2023
    Elevated constitutive expression of Hsp40 chaperone Sis1 reduces TDP-43 aggregation-induced oxidative stress in Ire1 pathway dependent-manner in yeast TDP-43 proteinopathy model of amyotrophic lateral sclerosis.

    Elevated constitutive expression of Hsp40 chaperone Sis1 reduces TDP-43 aggregation-induced oxidative stress in Ire1 pathway dependent-manner in yeast TDP-43 proteinopathy model of amyotrophic lateral sclerosis.
    Bharathi V, Bajpai A, Parappuram IT, Patel BK.

    03/19/2022
    Cysteine cross-linking in native membranes establishes the transmembrane architecture of Ire1.

    Cysteine cross-linking in native membranes establishes the transmembrane architecture of Ire1.
    Väth K, Mattes C, Reinhard J, Covino R, Stumpf H, Hummer G, Ernst R., Free PMC Article

    10/23/2021
    Protomer alignment modulates specificity of RNA substrate recognition by Ire1.

    Protomer alignment modulates specificity of RNA substrate recognition by Ire1.
    Li W, Crotty K, Garrido Ruiz D, Voorhies M, Rivera C, Sil A, Mullins RD, Jacobson MP, Peschek J, Walter P., Free PMC Article

    10/23/2021
    Vps34 and TOR Kinases Coordinate HAC1 mRNA Translation in the Presence or Absence of Ire1-Dependent Splicing.

    Vps34 and TOR Kinases Coordinate HAC1 mRNA Translation in the Presence or Absence of Ire1-Dependent Splicing.
    Uppala JK, Bhattacharjee S, Dey M., Free PMC Article

    07/24/2021
    Stress sensor Ire1 deploys a divergent transcriptional program in response to lipid bilayer stress.

    Stress sensor Ire1 deploys a divergent transcriptional program in response to lipid bilayer stress.
    Ho N, Yap WS, Xu J, Wu H, Koh JH, Goh WWB, George B, Chong SC, Taubert S, Thibault G., Free PMC Article

    03/20/2021
    Unfolded protein response (UPR) is subject to inhibition by oxidative stress. Inhibition is mediated by a single evolutionarily conserved cysteine in Ire1, and affects both luminal and membrane pathways of Ire1 activation.

    Regulation of the unfolded protein response in yeast by oxidative stress.
    Guerra-Moreno A, Ang J, Welsch H, Jochem M, Hanna J., Free PMC Article

    06/6/2020
    Endoplasmic reticulum stress causes a diminished mRNA decay, thus resulting in the production of a population with an increased abundance of pre-HAC1 mRNA carrying an intact bipartite element, which facilitates its more efficient recruitment to Ire1p foci.

    Nuclear mRNA degradation tunes the gain of the unfolded protein response in Saccharomyces cerevisiae.
    Sarkar D, Paira S, Das B., Free PMC Article

    07/6/2019
    The most conserved transducer of ER stress, Ire1, uses an amphipathic helix to sense membrane aberrancies and control unfolded protein response activity.

    Activation of the Unfolded Protein Response by Lipid Bilayer Stress.
    Halbleib K, Pesek K, Covino R, Hofbauer HF, Wunnicke D, Hänelt I, Hummer G, Ernst R.

    09/30/2017
    the AMPK Snf1p and ER stress kinase Ire1p regulated the HOG pathway.

    Metabolic respiration induces AMPK- and Ire1p-dependent activation of the p38-Type HOG MAPK pathway.
    Adhikari H, Cullen PJ., Free PMC Article

    07/4/2015
    Here we show that in yeast cells, the ER-stress sensor Ire1 was activated upon zinc deficiency

    Zinc depletion activates the endoplasmic reticulum-stress sensor Ire1 via pleiotropic mechanisms.
    Nguyen TS, Kohno K, Kimata Y.

    02/15/2014
    Deletion of MYO1 impairs the cluster formation of Ire1.

    F-actin and a type-II myosin are required for efficient clustering of the ER stress sensor Ire1.
    Ishiwata-Kimata Y, Yamamoto YH, Takizawa K, Kohno K, Kimata Y.

    11/2/2013
    Under ER stress, Ire1 molecules exist in activated and Bip-associated state.

    BiP-bound and nonclustered mode of Ire1 evokes a weak but sustained unfolded protein response.
    Ishiwata-Kimata Y, Promlek T, Kohno K, Kimata Y.

    09/7/2013
    Results show that the kinase domain autophosphorylatse the auto-inhibitory region in order to relieve auto-inhibition and that ADP acts as a switch to activate the kinase extension nuclease domain-catalyzed HAC1 mRNA cleavage.

    An ire1-phk1 chimera reveals a dispensable role of autokinase activity in endoplasmic reticulum stress response.
    Mannan MA, Shadrick WR, Biener G, Shin BS, Anshu A, Raicu V, Frick DN, Dey M.

    08/3/2013
    the cytosolic or transmembrane domain of Ire1 senses membrane aberrancy

    Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways.
    Promlek T, Ishiwata-Kimata Y, Shido M, Sakuramoto M, Kohno K, Kimata Y., Free PMC Article

    01/14/2012
    core ER-lumenal domain (cLD) of Ire1 binds to unfolded proteins in yeast and to peptides in vitro; peptide binding caused Ire1 cLD oligomerization in vitro, suggesting direct binding to unfolded proteins activates unfolded protein response

    Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response.
    Gardner BM, Walter P., Free PMC Article

    10/22/2011
    Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1.

    Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1.
    Wiseman RL, Zhang Y, Lee KP, Harding HP, Haynes CM, Price J, Sicheri F, Ron D., Free PMC Article

    05/31/2010
    oligomerization is central to Ire1 function and is an intrinsic attribute of its cytosolic domains; 3.2-A crystal structure of the oligomer of the Ire1 cytosolic domains in complex with a kinase inhibitor

    The unfolded protein response signals through high-order assembly of Ire1.
    Korennykh AV, Egea PF, Korostelev AA, Finer-Moore J, Zhang C, Shokat KM, Stroud RM, Walter P., Free PMC Article

    01/21/2010
    We have determined the crystal structure of the dual catalytic region of Ire1at 2.4 A resolution, revealing the fusion of a domain, which we term the KEN domain, to the protein kinase domain.

    Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing.
    Lee KP, Dey M, Neculai D, Cao C, Dever TE, Sicheri F., Free PMC Article

    01/21/2010
    Upon endoplasmic reticulum (ER) stress, Ire1 clusters and actually interacts with unfolded proteins.

    Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins.
    Kimata Y, Ishiwata-Kimata Y, Ito T, Hirata A, Suzuki T, Oikawa D, Takeuchi M, Kohno K., Free PMC Article

    01/21/2010
    Observations indicate that in addition to BiP dissociation and self-association of Ire1, another unknown change on the luminal side is crucial for Ire1 activation.

    Self-association and BiP dissociation are not sufficient for activation of the ER stress sensor Ire1.
    Oikawa D, Kimata Y, Kohno K.

    01/21/2010
    The capacity of a highly basic sequence in the linker region of Ire1p to function as a nuclear localization sequence (NLS) both in vivo and in vitro, was analyzed.

    The unfolded protein response transducer Ire1p contains a nuclear localization sequence recognized by multiple beta importins.
    Goffin L, Vodala S, Fraser C, Ryan J, Timms M, Meusburger S, Catimel B, Nice EC, Silver PA, Xiao CY, Jans DA, Gething MJ., Free PMC Article

    01/21/2010
    Our results are consistent with de-phosphorylation of Ire1 being a mechanism for antagonizing UPR signalling.

    Dcr2 targets Ire1 and downregulates the unfolded protein response in Saccharomyces cerevisiae.
    Guo J, Polymenis M., Free PMC Article

    01/21/2010
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