Fibroblast growth factor induces dephosphorylation and inactivation of the NPR2 guanylyl cyclase, thus decreasing cyclic GMP production in growth plate chondrocytes and contributing to FGF-dependent decreases in bone growth.
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.
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.
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.
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.
Nucleolar protein localization involves the phase separation within the nucleolar matrix via three types of multivalent features: acidic tracts, nucleic acid binding domains and arginine-rich low complexity sequences.
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.
Interactions between Neuropilin-1 and VEGFR2, rather than VEGF-Neuropilin-1 binding, underlie Neuropilin-1's critical function in VEGF-mediated vascular development.
