Publication: Domain compatibility in Ire1 kinase is critical for the unfolded protein response
2
Issued Date
2010-07-01
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ISSN
00145793
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2-s2.0-77954175676
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Mahidol University
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SCOPUS
Bibliographic Citation
FEBS Letters. Vol.584, No.14 (2010), 3203-3208
Suggested Citation
Juthakorn Poothong, Pattarawut Sopha, Randal J. Kaufman, Witoon Tirasophon Domain compatibility in Ire1 kinase is critical for the unfolded protein response. FEBS Letters. Vol.584, No.14 (2010), 3203-3208. doi:10.1016/j.febslet.2010.06.003 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/28675
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Title
Domain compatibility in Ire1 kinase is critical for the unfolded protein response
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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. © 2010 Federation of European Biochemical Societies.