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Oligomerization of the transmembrane domain of IRE1α in SDS micelles.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Cho H,Lamarca R,Chan C

doi

10.1016/j.bbrc.2012.09.135

subject

Has Abstract

pub_date

2012-11-02 00:00:00

pages

764-7

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(12)01913-4

journal_volume

427

pub_type

杂志文章

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