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Biochem J. 2005 Oct 1;391(Pt 1):135-42.

An essential dimer-forming subregion of the endoplasmic reticulum stress sensor Ire1.

Author information

1
Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.

Abstract

The luminal domain of the type I transmembrane protein Ire1 senses endoplasmic reticulum stress by an undefined mechanism to up-regulate the signalling pathway for the unfolded protein response. Previously, we proposed that the luminal domain of yeast Ire1 is divided into five subregions, termed subregions I-V sequentially from the N-terminus. Ire1 lost activity when internal deletions of subregion II or IV were made. In the present paper, we show that partial proteolysis of a recombinant protein consisting of the Ire1 luminal domain suggests that subregions II-IV are tightly folded. We also show that a recombinant protein of subregions II-IV formed homodimers, and that this homodimer formation was impaired by an internal deletion of subregion IV. Furthermore, recombinant fragments of subregion IV exhibited a self-binding ability. Therefore, although its sequence is little conserved evolutionarily, subregion IV plays an essential role to promote Ire1 dimer formation.

PMID:
15954865
PMCID:
PMC1237147
DOI:
10.1042/BJ20050640
[Indexed for MEDLINE]
Free PMC Article

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