Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
Membrane transport is the means by which small molecules and biopolymers permeate a cell membrane. Membranes are lipid bilayers exhibiting selective permeability, meaning that they are permeable to some substances and not to others. Membrane transport is mediated by membrane-transport proteins.
A clear picture of how and why cells inevitably lose viability is still lacking. A dynamical systems view of starving bacteria points to a continuous energy expenditure needed for maintaining the right osmotic pressure as an important factor.
Human multidrug resistance protein 5 (hMRP5) effluxes anticancer and antivirus drugs, driving multidrug resistance. Here, the authors present cryo-EM structures of hMRP5 in different states, showing that hMRP5 can be autoinhibited by a short peptide from its N-terminal tail, which prevents the entry of substrates into hMRP5’s transport pathway.
Intracellular potassium (K+) homeostasis is achieved by activity of both ion channels and transporters. Here, the authors report structures of E. coli glutathione (GSH)-gated K+ efflux transporter KefC with bound K+ and conclude that the ion-binding site is adapted for binding a dehydrated ion.
Efflux pumps confer antibiotic resistance by coupling proton import with drug export. In this work, the authors uncover the proton-coupled transport mechanism for the clinically relevant efflux pump NorA from the pathogenic bacterium S. aureus.
Sialin transports multiple substrates including sialic acid out of lysosomes, and neurotransmitters into synaptic vesicles. This study reports the cryo-EM structures of Sialin in multiple states revealing its transport and pH-sensing mechanisms.
Structures of the kainate receptor GluK2 with and without concanavilin A and BPAM344 show how these ligands modulate channel activity and reveal the molecular basis of kainate receptor gating.
Skeletal ryanodine receptor controls calcium mobilization indispensable for muscle contraction. Here, authors combine cryo-EM and molecular dynamics to uncover the structural basis of the intricate regulation of this channel by calcium and magnesium.
A clear picture of how and why cells inevitably lose viability is still lacking. A dynamical systems view of starving bacteria points to a continuous energy expenditure needed for maintaining the right osmotic pressure as an important factor.
In this work, Morgenstern and colleagues describe an approach involving functionalized nanobodies which decrease the activity of voltage-gated Ca2+ channels associated with β1 subunits and promote their removal from the surface membrane of neurons and muscle.
Using organic solvent shortens formation time of membrane nanosheets comprising proteins and copolymers, while tuning protein structure tailors the pore geometry, resulting in superior water permeation.
Cellular organelles extensively communicate with each other by close interactions, known as membrane contact sites. Schuldiner and Bohnert comment on the progress of this rapidly developing field, highlighting that the complexity of interactions at membrane contact sites is only now starting to emerge.