Oligomerization of the transmembrane domain of IRE1α in SDS micelles

Hyunju Cho, Ryan LaMarca, Christina Chan

    Research output: Research - peer-reviewArticle

    • 2 Citations

    Abstract

    IRE1α (Inositol-requiring enzyme 1 α), an endoplasmic reticulum (ER)-resident sensor for mammalian unfolded protein response, is a type I transmembrane protein which has a bifunctional enzyme containing kinase and RNase domains. Although the luminal domain and cytosolic domain of IRE1α are thought to play crucial roles in regulating the protein activity, no functional and structural studies of the transmembrane domain exist thus far. Herein, using CD spectroscopy, we report that the transmembrane domain of the IRE1α is alpha-helical in a membrane-like environment. In addition, SDS-PAGE and FRET analyses support that the transmembrane domain forms oligomers in SDS micelles. Thus, the study would provide insights into how the transmembrane domain plays a role in regulating the IRE1α protein activity.

    LanguageEnglish (US)
    Pages764-767
    Number of pages4
    JournalBiochemical and Biophysical Research Communications
    Volume427
    Issue number4
    DOIs
    StatePublished - Nov 2 2012

    Profile

    Micelles
    Proteins
    Oligomerization
    Enzymes
    Unfolded Protein Response
    Inositol
    Ribonucleases
    Endoplasmic Reticulum
    Polyacrylamide Gel Electrophoresis
    Spectrum Analysis
    Phosphotransferases
    Membranes
    Oligomers
    Spectroscopy
    Sensors

    Keywords

    • Dimerization
    • Endoplasmic reticulum
    • IRE1α
    • Transmembrane domain

    ASJC Scopus subject areas

    • Biochemistry
    • Biophysics
    • Cell Biology
    • Molecular Biology

    Cite this

    Oligomerization of the transmembrane domain of IRE1α in SDS micelles. / Cho, Hyunju; LaMarca, Ryan; Chan, Christina.

    In: Biochemical and Biophysical Research Communications, Vol. 427, No. 4, 02.11.2012, p. 764-767.

    Research output: Research - peer-reviewArticle

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