Oligomerization of the transmembrane domain of IRE1α in SDS micelles

Hyunju Cho, Ryan LaMarca, Christina Chan

Research output: Contribution to journalArticle

  • 3 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

Oligomerization
Micelles
Unfolded Protein Response
Proteins
Inositol
Enzymes
Ribonucleases
Endoplasmic Reticulum
Polyacrylamide Gel Electrophoresis
Spectrum Analysis
Phosphotransferases
Oligomers
Membranes
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: Contribution to journalArticle

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