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Bingdong Sha on Muck Rack

Bingdong Sha

As seen in: The Journal of Biological Chemistry
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Articles

The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization

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By Peng Wang, Jingzhi Li, Jiahui Tao, Bingdong Sha
| The Journal of Biological Chemistry Verified
PRKR-like endoplasmic reticulum kinase (PERK) is one of the major sensor proteins that detect protein folding imbalances during endoplasmic reticulum (ER) stress. However, it remains unclear how ER stress activates PERK to initiate a downstream unfolded protein response (UPR). Here, we found that PERK's luminal domain can recognize and selectively interact with misfolded proteins but not with native proteins.
Open in Who Shared Issue with article?

The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization

|
By Peng Wang, Jingzhi Li, Jiahui Tao, Bingdong Sha
| The Journal of Biological Chemistry Verified
PRKR-like endoplasmic reticulum kinase (PERK) is one of the major sensor proteins that detect protein folding imbalances during endoplasmic reticulum (ER) stress. However, it remains unclear how ER stress activates PERK to initiate a downstream unfolded protein response (UPR). Here, we found that PERK’s luminal domain can recognize and selectively interact with misfolded proteins but not with native proteins.
Open in Who Shared Issue with article?
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