Abstract
The long-awaited structure of the effector portion of IRE1, the endoplasmic reticulum stress transducer, is published in this issue of Cell (Lee et al., 2008). This structure provides new insight into the mysterious coupling of kinase and endoribonuclease activities in the oldest, most-conserved branch of the unfolded protein response in eukaryotes.
MeSH terms
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Alternative Splicing / physiology
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Catalytic Domain / physiology
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Endoplasmic Reticulum / metabolism*
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Endoplasmic Reticulum / ultrastructure
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Endoribonucleases / chemistry
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Endoribonucleases / genetics
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Endoribonucleases / metabolism
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Membrane Glycoproteins / chemistry*
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Membrane Glycoproteins / genetics
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Membrane Glycoproteins / metabolism
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Oxidative Stress / physiology*
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Phosphotransferases / chemistry
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Phosphotransferases / genetics
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Phosphotransferases / metabolism
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Protein Serine-Threonine Kinases / chemistry*
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Protein Serine-Threonine Kinases / genetics
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Protein Serine-Threonine Kinases / metabolism
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Protein Structure, Tertiary / physiology
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Saccharomyces cerevisiae Proteins / chemistry*
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism
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Yeasts / metabolism*
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Yeasts / ultrastructure
Substances
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Membrane Glycoproteins
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Saccharomyces cerevisiae Proteins
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Phosphotransferases
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IRE1 protein, S cerevisiae
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Protein Serine-Threonine Kinases
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Endoribonucleases