FEBS Letters
Volume 582, Issue 5 , Pages 656-660, 5 March 2008

RNase domains determine the functional difference between IRE1α and IRE1β

Edited by Robert Barouki

  • Yusuke Imagawa

      Affiliations

    • Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma 630-0192, Japan
    • ,
  • Akira Hosoda

      Affiliations

    • Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma 630-0192, Japan
    • Iwawaki Initiative Research Unit, RIKEN, Wako 351-0198, Japan
    • ,
  • Shin-ichi Sasaka

      Affiliations

    • Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma 630-0192, Japan
    • ,
  • Akio Tsuru

      Affiliations

    • Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma 630-0192, Japan
    • ,
  • Kenji Kohno

      Affiliations

    • Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma 630-0192, Japan
    • Corresponding Author InformationCorresponding author. Fax: +81 743 72 5649.

Received 28 November 2007; received in revised form 21 January 2008; accepted 23 January 2008. published online 31 January 2008.

Abstract 

Endoplasmic reticulum (ER) stress is associated with the functional disorder of the ER. During conditions of ER stress, cells induce at least two responses to maintain ER function: transcriptional upregulation of ER quality control genes, and translational attenuation of protein synthesis. Induction of ER quality control proteins is mediated by IRE1α, which activates the transcription factor XBP1 via an unconventional splicing event, while a partial translational attenuation is mediated by IRE1β. Here, we show by both in vivo and in vitro analyses that the RNase domain of IRE1 determines the functional specificities of each of these isoforms.

Abbreviations: aa, amino acid, ER, endoplasmic reticulum, hIRE1, human IRE1, rIRE1, recombinant hIRE1 protein, RNase, endoribonuclease, Tm, tunicamycin, UPR, unfolded protein response

Keywords: ER stress, IRE1, Unfolded protein response

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PII: S0014-5793(08)00061-6

doi:10.1016/j.febslet.2008.01.038

FEBS Letters
Volume 582, Issue 5 , Pages 656-660, 5 March 2008

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