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 conformational mechanism of a transporter protein is found to have profound and energetically costly effects on the morphology of the surrounding membrane.
The crystal structure of a ternary complex of a TonB-dependent transporter containing a signalling domain, bound to siderophore as well as TonB, provides mechanistic insights into siderophore uptake and signalling.
Auxiliary proteins play functional roles in modulating the assembly and activity of a non-canonical ABC transporter that is important for the maintenance of outer membrane lipid asymmetry.
Evolutionary bioinformatics and experimentation are applied to the components of the Tat protein transport system to elucidate the structure of the membrane-bound receptor complex and to deduce a molecular description for its substrate-triggered activation.
During cilium-generated signaling, ciliary membrane protein trafficking is unidirectional and ciliary membrane protein composition is regulated through action in the cytoplasm of the retrograde intraflagelllar transport (IFT) motor and shedding of ciliary ectosomes.
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.
Crystal structures provide structural rationales for the transport stoichiometry of the gastric proton pump, which suffices the energy requirement for the generation of a million-fold proton gradient across the membrane.
In Drosophila oocytes, the exclusion of the scaffold protein PAR3 from the posterior cortex depends on PAR1 and endocytosis, while its anterior localisation requires microtubules and recycling endosomes.
