FEBS Lett. 2010 Jul 16;584(14):3203-8. doi: 10.1016/j.febslet.2010.06.003. Epub 2010 Jun 10.

Domain compatibility in Ire1 kinase is critical for the unfolded protein response.

Poothong J, Sopha P, Kaufman RJ, Tirasophon W.

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The Institute of Molecular Biosciences, Mahidol University, Salaya, Nakhon Pathom, Thailand.

Abstract

The unfolded protein response is a mechanism to cope with endoplasmic reticulum stress. In Saccharomyces cerevisiae, Ire1 senses the stress and mediates a signaling cascade to upregulate responsive genes through an unusual HAC1 mRNA splicing. The splicing requires interconnected activity (kinase and endoribonuclease (RNase)) of Ire1 to cleave HAC1 mRNA at the non-canonical splice sites before translation into Hac1 transcription factor. Analysis of the truncated kinase domain from Ire1 homologs revealed that this domain is highly conserved. Characterization by domain swapping indicated that a functional ATP/ADP binding domain is minimally required. However the overall domain compatibility is critical for eliciting its full RNase function.

PMID:: 20541549; [PubMed - indexed for MEDLINE]

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Cited by 1 PubMed Central article

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Domain compatibility in Ire1 kinase is critical for the unfolded protein respons...
Domain compatibility in Ire1 kinase is critical for the unfolded protein response.
FEBS Lett. 2010 Jul 16 ;584(14):3203-8. doi: 10.1016/j.febslet.2010.06.003. Epub 2010 Jun 10 .

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