The human cytomegalovirus (HCMV) interactome systematically characterises high-confidence viral-viral and viral-host protein interactions in HCMV-infected cells, facilitating multiple novel insights into HCMV and herpesviral function.
A new mitochondrial protein degradation pathway selectively sorts and destroys a subset of the mitochondrial membrane proteome to protect mitochondria in times of stress.
Proteasomes are protected from autophagic elimination upon carbon starvation by sequestration into cytoplasmic storage granules, which aid cell fitness by providing a cache of proteasomes that can be rapidly remobilized when carbon availability improves.
Doa10, a membrane-embedded ubiquitin ligase, facilitates the removal of membrane proteins from the endoplasmic reticulum and cooperates with the Cdc48 ATPase in this process.
Mechanical loading and the bone anabolic action of parathyroid hormone result in rapid, lysosomal degradation of sclerostin protein, revealing physiologically important post-translational control of this critical regulator of bone formation.
Under normal nutritional conditions, G-protein coupled receptors can control autophagy by regulating the degradation of key autophagic regulator Atg14L through ZBTB16-mediated ubiquitination and proteasome degradation.
Retrieval enhances fear memory through reconsolidation by activating calcineurin-induced protein degradation and CREB-mediated gene expression in amygdala, hippocampus, and mPFC.
Dynamic SILAC labeling in combination with mass spectrometry revealed substantial regulation of protein synthesis, degradation, turnover, and abundance during homeostatic scaling in neurons.
