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.
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.
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.
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.
Building on previous work (De Michele et al., 2013), we report the development of dual-emission AmTrac sensors for in vivo analysis of transporter activity.
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.
A new family of sterol-specific lipid transfer proteins has been found that anchors in the endoplasmic reticulum; some of these proteins stretch across membrane contacts and mediate sterol traffic from the plasma membrane.
LPCAT3 incorporates arachidonic acid into membrane phospholipids, which promotes lipoprotein assembly by enabling triacylgylcerols to cluster in the membrane.
A structure of the complete, membrane bound, COPII coat solved by sub-tomogram averaging reveals the arrangement of all protein subunits on the membrane and suggests a mechanism for coating heterogeneously-shaped carriers.
