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

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

Transcription factors KLF2 and ETV1 repress the transcriptional program of mitochondrial biogenesis, resulting in impaired mitochondrial function in lysosomal storage diseases.

LAMP proteins, the major glycoproteins of the lysosome membrane, bind cholesterol directly and specifically, and interact with NPC1 and NPC2 proteins as part of the lysosomal cholesterol export process.

The endo-lysosomal system plays a positive essential role in the initiation of the cell cycle in yeast.

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

Impaired lysosomal acidification results in retention of iron inside lysosomes, triggering functional iron deficiency, dysfunctional mitochondria (especially mtDNA loss), and inflammation in vivo in a mouse model of lysosomal disease.

Tricyclic antidepressants activate lysosomal two-pore Na⁺ channels in a voltage-dependent manner.

The N-terminal domain of one NPC1 molecule can transfer its cholesterol to another NPC1 molecule lacking the N-terminal domain, suggesting that NPC1 forms multimers that transport cholesterol out of lysosomes.

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