COPII vesicles regulate the metabolism of cholesterol through the selective transport of secretory proteins.

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.

We challenge a recent report that most of the cholesterol in the plasma membrane of mammalian cells is in the exofacial leaflet.

The activation and membrane localization of the broadly-tuned noxious chemosensory cation channel TRPA1 are regulated by direct interactions with cholesterol via CRAC motifs in transmembane segments 2 and 4.

A post-lysosomal cholesterol transport inhibitor reveals how the endoplasmic reticulum membrane regulates total cellular cholesterol by constantly monitoring a critical pool of cholesterol in the plasma membrane.

The integral membrane protein LucA facilitates fatty acid and cholesterol uptake into Mycobacterium tuberculosis by stabilizing the Mce1 and Mce4 transporters, respectively, and Mce1 functions as a fatty acid transporter in Mycobacterium tuberculosis.

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.

Precise control of cellular cholesterol levels is achieved by organization of cholesterol into three distinct pools in the plasma membrane.

Accessible cholesterol levels in human red blood cells were found to be stable within individuals but vary >10-fold among individuals and this variability may contribute to differences in cholesterol trafficking among tissues.

A nanomolar inhibitor of cholesterol transport out of endosomes/lysosomes can be crosslinked to the “sterol-sensing domain” of NPC1, which implicates this domain in the transmembrane transport of cholesterol.