A method for determining how many ions are required to drive transport in an electrogenic secondary active transporter will help understand the mechanisms of bacterial transporters whose structures have been solved.

High affinity interactions with transport adaptors are important to shield the interaction surfaces of cytomatrix components to block fatal premature oligomerization of active zone proteins during axonal transport.

A simple model of active transport in neurons allows intracellular cargo to find sites of demand using only local signals, but predicts long delays in distributing cargo throughout a dendritic tree.

Potassium presumably binds to the Na1 site in LeuT, playing a role in inwardly rectifying the transport of substrates.

The structure of the membrane-integrated components of a unique substrate decarboxylation-driven primary-active sodium pump provides insights into its transport mechanism.

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.

The Ran GTPase plays a role in defining the physical properties of the nuclear pore complex transport channel by remodeling the binding interactions of importin-β with the nucleoporin Nup153 at the nuclear face of the pore.

The conformational dynamics of multidrug resistance protein 1 (MRP1) are tracked in real time by single-molecule fluorescence resonance energy transfer experiments, which elucidate the rate-limiting mechanism of MRP1's transport cycle.

The inward-open and outward-open structures of MjNhaP1 explain the mechanism of electroneutral sodium-proton antiport across the cell membrane.