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

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

Dysfunction and overexpression of ENaC-mediated sodium influx exacerbates activation of NLRP3-inflammasome mediated inflammation in cells with CF-associated mutations and is modulated by inhibition of these amiloride-sensitive sodium (Na⁺) channels.

In potassium-dependent NTPases, insertion of the activating potassium ion into the active site leads to rotation of the gamma-phosphate yielding a near-eclipsed, catalytically productive conformation of the triphosphate chain.

The X-ray structure of the PaNhaP provides a unique view of substrate-ion binding and release in electroneutral sodium/proton antiporters.

Sodium ions control the rates of both substrate binding and dissociation of an archaeal homologue of glutamate transporters in a manner that minimizes binding intermediates and maximizes transport efficiency.

Sodium ions but not protons induce defined helix movements in a sodium/proton antiporter and suggest a mechanism for Na + binding and transport.

Transient Ca elevations of cytoplasmic calcium in cardiac myocytes profoundly activate cardiac Na/K pump activity in parallel with physical-chemical changes of the sarcolemma but without involvement of conventional signaling mechanisms.

The structures of the bovine and human BBSome reveal that a conformational change is required to recruit the complex to the ciliary membrane.

The way that bacteria grow—either floating in liquid or attached to a surface—affects their ability to evolve antimicrobial resistance and our ability to treat infections.