What question did this study set out to answer?

To elucidate how the signal transducer Ire1 senses endoplasmic reticulum (ER) stress and becomes activated.

October 8, 2007The Journal of Cell BiologyOpen Access

Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins

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Authors

YKYukio KimataNara Institute of Science and Technology YIYuki Ishiwata‐KimataNara Institute of Science and Technology TITatsuhiko ItoUniversity of Fukui

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Implication

Mechanistic study reveals two-step Ire1 activation driven by BiP release and unfolded protein binding, demonstrating how cells sense endoplasmic reticulum stress.

Key Points

To elucidate how the signal transducer Ire1 senses endoplasmic reticulum (ER) stress and becomes activated.
Examined Ire1 cluster formation and its direct interaction with unfolded proteins during ER stress conditions.
Engineered and analyzed specific Ire1 mutations to dissect discrete stages of receptor activation.
Showed that ER stress induces Ire1 to form higher-order clusters and physically bind to unfolded proteins.
Identified a two-step activation mechanism where BiP dissociation first promotes Ire1 clustering, after which unfolded protein binding to the core stress-sensing region (CSSR) reorients cytosolic effector domains.

Cite This Study

Kimata et al. (2007) studied this question.

synapsesocial.com/papers/6a7118edf44fa9f079dedead https://doi.org/10.1083/jcb.200704166

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Implication

Mechanistic study reveals two-step Ire1 activation driven by BiP release and unfolded protein binding, demonstrating how cells sense endoplasmic reticulum stress.

Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins

Discussion

Member takes

Implication

Key Points

Cite This Study

Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins

Discussion

Member takes

Implication

Key Points

Cite This Study

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