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Protein folding is the process by which proteins achieve their mature functional (native) tertiary structure, and often begins co-translationally. Protein folding requires chaperones and often involves stepwise establishment of regular secondary and supersecondary structures, namely α-helices and β-sheets, that fold rapidly, stabilized by hydrogen bonding and disulphide bridges, and then tertiary structure.
Sensing stress within the endoplasmic reticulum (ER), the ER transmembrane protein IRE1α initiates a signal transduction pathway to restore homeostasis. A study finds that this process requires an ER membrane-bound phase separation event that leads to the local assembly of stress granules (SGs) and delivery of signalling components.
Here the authors connect inherited Apolipoprotein E genotype with the risk of developing Alzheimer’s disease by demonstrating how, in an isoform- and lipidation-specific way, apoE modulates the aggregation, clearance and toxicity of Amyloid-beta.
In this Perspective, the authors propose a framework to explain membrane protein biogenesis, wherein different parts of a nascent substrate are triaged between Oxa1 and SecY family members for insertion.
Sensing stress within the endoplasmic reticulum (ER), the ER transmembrane protein IRE1α initiates a signal transduction pathway to restore homeostasis. A study finds that this process requires an ER membrane-bound phase separation event that leads to the local assembly of stress granules (SGs) and delivery of signalling components.
Claire Durrant reminds us of the importance of studying the physiological roles of proteins and their aggregates to understand their roles in disease and inform therapies, discussing a 2008 paper on amyloid-β from the Arancio lab.
Natural protein folding takes place in aqueous cell environments. Now, it has been found that proteins in a water-free environment undergo faster and more efficient folding.