期刊
BIOCHEMICAL JOURNAL
卷 391, 期 -, 页码 135-142出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20050640
关键词
endoplasmic reticulum chaperone; immunoglobulin heavy-chain binding protein (BiP)/78 kDa glucose-regulated protein (GRP78); Irel; partial proteolysis; stress sensor; unfolded protein response (UPR)
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.
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