A new mitochondrial protein degradation pathway selectively sorts and destroys a subset of the mitochondrial membrane proteome to protect mitochondria in times of stress.

The endoplasmic reticulum serves as a direct and primary source of calcium ions for the lysosome.

Emerin, a protein that plays key roles in nuclear organization, can be dynamically degraded in response to environmental stimuli such as ER stress.

The AAA-ATPase VCP sustains sarcoplasmic proteostasis, in part, by controlling autophagosome-lysosome fusion and the integrity of a dynamic tubular lysosomal network.

Disruption of TFEB and TFE3 results in diminished p53 signaling capacity and altered cell cycle regulation under genotoxic stress conditions.

The pseudoenzyme CPT1C is able to sense changes in intracellular malonyl-CoA levels caused by nutrients or energy stress and regulate late endosomes/lysosomes anterograde transport, necessary for proper axon growth.

In neuronal mitophagy, Parkin and OPTN induce efficient sequestration of damaged somal mitochondria into autophagosomes, but slow turnover via lysosomal acidification may be a point of vulnerability for the cell.

The organic insecticide spinosad severely impacts metabolism, the cell biology, and the visual system of the model insect Drosophila, suggesting that it poses a threat to other non-pest insect exposed to it in the field.

ER-resident chaperones and cargo receptors make excursions to the cell surface and endocytic compartments when they accompany misfolded clients to lysosomes for degradation.

Lysosomes are highly enriched in chloride, which is essential for their degradative function.