The conformational mechanism of a transporter protein is found to have profound and energetically costly effects on the morphology of the surrounding membrane.

Electron tomography and biochemical approaches demonstrate a direct role for WDR35, beyond integrity of the IFT-A holocomplex, in the formation and fusion of electron-dense-coated vesicles to the ciliary sheath and pocket for delivery of cargos necessary for axoneme elongation.

An Acinetobacter baumannii ABC transporter likely facilitates transport of glycerophospholipids from the inner to the outer 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.

Staphylococcal heme acquisition needs a highly structured cell envelope, the membrane transporter accumulates in membrane domains most likely to allow concerted passage of heme from the cell wall-funnel to the 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.

Emerin, a protein that plays key roles in nuclear organization, can be dynamically degraded in response to environmental stimuli such as ER stress.

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 high-resolution x-ray structure of an asymmetrical SeCitS dimer, present in the inward- and outward-facing state, provides a complete mechanism of substrate and ion translocation in a sodium-dependent symporter.

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.