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Biomedical Basics

ER stress and UPR (unfolded protein response)

  • Created by Henry Stewart Talks
Published on May 28, 2026   4 min

A selection of talks on Cell Biology

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In this talk, the focus is ER stress and UPR, unfolded protein response, supported by coverage of the essential roles of the endoplasmic reticulum in protein folding and quality control, and how disruptions lead to ER stress and activation of the unfolded protein response. We will examine the molecular components and pathways that detect and respond to misfolded proteins, including the roles of IRE one, PRC, and ATF six. The consequences of persistent ER stress, including its links to diseases such as neurodegeneration and diabetes, will be discussed. Finally, we will explore emerging therapeutic strategies that target the UPR to treat these conditions. The endoplasmic reticulum or ER is essential for synthesizing, folding and maturing proteins destined for secretion or membrane residency. Newly synthesized polypeptides must fold into correct three dimensional structures with help from molecular chaperones, like BIP, calnexin and articulin and enzymes for modifications such as disulfide bond formation. Disruptions like high protein demand or stress, cause ER stress, triggering the unfolded protein response or UPR. If this balance is not restored, serious cellular consequences can occur. When misfolded proteins accumulate in the ER, molecular chaperones and quality control systems initially manage them. If overwhelmed, ER stress triggers the UPR,

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ER stress and UPR (unfolded protein response)

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