Activating the Unfolded Protein Response: PERK-ATF4 Signaling
Description
This template was adapted from the original submission. Edits were made to enhance scientific accuracy, optimal usability and/or to meet industry-leading design standards for science communication.
Intracellular sensors located at the ER membrane detect misfolded proteins and elicit a cellular response. The dissociation of BiP following the interaction with misfolded proteins leads to the dimerization of PERK (protein kinase R (PKR)-like endoplasmic reticulum kinase) and its activation by autophosphorylation. PERK subsequently activates eIF2a, driving an imbalance in the translational machinery that leads to the selective translation of ATF4.
Acknowledgements
References
Bertolotti, A. (2000) Dynamic interaction of BiP and ER stress transducers in the unfolded- protein response. Nature Cell Biology. http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=10854322%5Cnhttp://www.nature.com/cgi-taf/DynaPage.taf?file=/ncb/journal/v2/n6/full/ncb0600_326.html%5Cnhttp://www.nature.com/cgi-taf/DynaPage.taf?file=/ncb/journal/v2/n6/abs/ncb06
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