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.

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.

Diversification of a conserved cholesterol binder drives functional replacement of cholesterol with symbiont-produced sterols in corals living in nutrient-poor environments.

NPC1 is a genetic determinant of filovirus susceptibility in bats, and some variations in bat NPC1 may reflect host adaptations to reduce filovirus replication and virulence.

Discovery of how cells couple addition of membranes with insertion of nuclear pore complexes to form and grow the nucleus.

Molecular analysis of cholesterol transport by NPC1 and NPC1L1 proteins reveals that cholesterol likely moves through these transporters, and ezetimibe blocks NPC1L1 by binding at the interface between multiple domains.

Expression of plant immune genes is controlled by the opposing actions of ubiquitin ligases and deubiquitinases that modify the master coactivator NPR1, thereby regulating its intrinsic transcriptional activity.

Sterol transport by Niemann-Pick type C proteins induces the expansion of raft-like domains in the yeast vacuole, enabling engulfment of lipid droplets by microautophagy.

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.