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.

Messenger RNA degradation alters protein trafficking to control transcription.

Retrieval enhances fear memory through reconsolidation by activating calcineurin-induced protein degradation and CREB-mediated gene expression in amygdala, hippocampus, and mPFC.

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.

Tom1 is the ubiquitin ligase in yeast that anchors a protein quality control pathway that rapidly eliminates ribosomal proteins that fail to assemble into ribosomes.

Mutations in an enzyme involved in protein degradation affect a signaling pathway that stimulates the development of the digestive tract.

The lysosome membrane is a new functional location for the ESCRTs in yeast.

Endoplasmic reticulum stress in yeast activates not only the UPR but also Rpn4, promoting the clearance of misfolded proteins from the cytosol as part of a modular cross-compartment stress response.