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

The time it takes to secrete a protein is dominated by diffusion of positively charged arginines through the channel across the membrane, but lysines avoid this problem as they are neutralised before transport.

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.

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.

Membrane receptor proteins move through primary cilia largely by passive diffusion rather than by active intraflagellar transport.

TANGO1 functions as a linactant filament to stabilize shallow COPII-coated buds, and after which membrane tension regulation, possibly mediated by TANGO1-controlled membrane fusion, facilitates bud elongation for procollagen export.

Structures of multiple states of two dicarboxylate transporters explain the conformational changes needed for substrate import.

A combination of cryo-electron microscopy, structure prediction, and evolutionary analyses reveal several functional states of the dynamic protein translocation machinery at the mammalian endoplasmic reticulum.

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.

Biochemical and cell-based analyses reveal how a non-enveloped virus exploits the chaperone activity of an ER transmembrane protein to penetrate the ER membrane required for successful virus infection.