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.

Macrophages release 30-nm vesicular particles enriched in accessible cholesterol during cellular locomotion, a discovery that is likely relevant to cholesterol disposal by these cells.

The patched hedgehog receptor inhibits the transmembrane transducer smoothened by reducing the accessibility of cholesterol locally at the membrane of the primary cilium.

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.

Sterol kinetics and cell-based assays reveal a heretofore unknown step in cholesterol trafficking through the endolysosomal compartment, involving a direct functional interaction between NPC2 and lysosbisphosphatidic acid.

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.