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.

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.

The so far uncharacterized lysosomal transporter protein MFSD1 is essential for liver homeostasis and needs the highly glycosylated GLMP protein as an accessory subunit for stability.

Dysfunctions of myelin peroxisomes cause a lysosomal storage-like disorder associated with alterations in glial and axonal membranes, which is the likely cause of nerve impairment in peroxisomal disorders.