The glucose-sensing transcription factor MondoA regulates zebrafish epiboly via cholesterol biosynthesis genes including the human disease gene Nsdhl, revealing an unknown role for metabolic glucose signalling in vertebrate development.
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.
GRAMD1 proteins sense a transient expansion of the accessible pool of plasma membrane cholesterol and facilitate its transport to the endoplasmic reticulum at ER-PM contact sites.
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.
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.
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.
The patched hedgehog receptor inhibits the transmembrane transducer smoothened by reducing the accessibility of cholesterol locally at the membrane of the primary cilium.
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.