The ability of epithelial cells to distinguish between domains on opposing cell surfaces within a tissue, a property known as planar cell polarity, relies on proteins and protein complexes directing the traffic of signaling proteins to specific locations on the cell surface membrane.

A transmembrane protein uses distinct mechanisms to regulate the movement of specific toll-like receptors-key immune system components involved in detecting pathogens-to their final locations inside cells.

A protein complex that enables cells to transport substances across their membranes, and that typically consists of four subunits, can also function as two hemicomplexes, each with two subunits.

COPII vesicles regulate the metabolism of cholesterol through the selective transport of secretory proteins.

The cisternae of the Golgi contain two functionally distinct domains: the central areas, which remain stationary, and the edges or rims, which are mobile.

Synergistic interactions with PI(4,5)P2 and activated Rho1, which are enriched at the apical membrane of tubular organs, facilitate tight apical targeting of the formin Diaphanous.

A cell-free biochemical assay for protein lipidation identifies the ER–Golgi intermediate compartment as a key early station in the formation of an autophagosome.

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.

Evidence that certain proteins can be transported between Golgi via structures that resemble COPI vesicles suggests that these vesicles could also be involved in the transport of proteins from the cis to the trans face of the Golgi.