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Activating the Unfolded Protein Response: PERK-ATF4 Signaling

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Angel Santiago-Lopez

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BioRender Team

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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.

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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.

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